Sortilin 1: Difference between revisions

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{{Infobox_gene}}
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'''Sortilin''' ('''SORT1''') is a [[protein]] that in humans is encoded by the ''SORT1'' [[gene]] on [[Chromosome 1 (human)|chromosome 1]].<ref name="entrez">{{cite web | title = Entrez Gene: SORT1 sortilin 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6272| accessdate = }}</ref> This protein is a type I membrane [[glycoprotein]] in the vacuolar protein sorting 10 protein (Vps10p) family of sorting receptors. While it is ubiquitously expressed in many tissues,<ref>{{Cite web|url=http://biogps.org/#goto=genereport&id=6272|title=BioGPS - your Gene Portal System|website=biogps.org|access-date=2016-08-16}}</ref> sortilin is most abundant in the [[central nervous system]].<ref name="ReferenceA">{{cite journal | vauthors = Andersen JL, Schrøder TJ, Christensen S, Strandbygård D, Pallesen LT, García-Alai MM, Lindberg S, Langgård M, Eskildsen JC, David L, Tagmose L, Simonsen KB, Maltas PJ, Rønn LC, de Jong IE, Malik IJ, Egebjerg J, Karlsson JJ, Uppalanchi S, Sakumudi DR, Eradi P, Watson SP, Thirup S | title = Identification of the first small-molecule ligand of the neuronal receptor sortilin and structure determination of the receptor-ligand complex | journal = Acta Crystallographica Section D | volume = 70 | issue = Pt 2 | pages = 451–60 | date = February 2014 | pmid = 24531479 | pmc = 3940197 | doi = 10.1107/S1399004713030149}}</ref> At the cellular level, sortilin functions in protein transport between the [[Golgi apparatus]], [[endosome]], [[lysosome]], and [[plasma membrane]], leading to its involvement in multiple biological processes such as [[Glucose metabolism|glucose]] and [[lipid metabolism]] as well as [[Nervous system|neural]] [[Human development (biology)|development]] and [[cell death]].<ref name=pmid11331584>{{cite journal | vauthors = Nielsen MS, Madsen P, Christensen EI, Nykjaer A, Gliemann J, Kasper D, Pohlmann R, Petersen CM | title = The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein | journal = The EMBO Journal | volume = 20 | issue = 9 | pages = 2180–90 | date = May 2001 | pmid = 11331584 | pmc = 125444 | doi = 10.1093/emboj/20.9.2180}}</ref><ref name=pmid23966466>{{cite journal | vauthors = Huang G, Buckler-Pena D, Nauta T, Singh M, Asmar A, Shi J, Kim JY, Kandror KV | title = Insulin responsiveness of glucose transporter 4 in 3T3-L1 cells depends on the presence of sortilin | journal = Molecular Biology of the Cell | volume = 24 | issue = 19 | pages = 3115–22 | date = October 2013 | pmid = 23966466 | pmc = 3784384 | doi = 10.1091/mbc.E12-10-0765}}</ref><ref name=pmid25593281>{{cite journal | vauthors = Patel KM, Strong A, Tohyama J, Jin X, Morales CR, Billheimer J, Millar J, Kruth H, Rader DJ | title = Macrophage sortilin promotes LDL uptake, foam cell formation, and atherosclerosis | journal = Circulation Research | volume = 116 | issue = 5 | pages = 789–96 | date = February 2015 | pmid = 25593281 | pmc = 4602371 | doi = 10.1161/CIRCRESAHA.116.305811}}</ref><ref name=pmid25702058>{{cite journal | vauthors = Kjolby M, Nielsen MS, Petersen CM | title = Sortilin, encoded by the cardiovascular risk gene SORT1, and its suggested functions in cardiovascular disease | journal = Current Atherosclerosis Reports | volume = 17 | issue = 4 | pages = 496 | date = April 2015 | pmid = 25702058 | doi = 10.1007/s11883-015-0496-7}}</ref><ref name=pmid14985763>{{cite journal | vauthors = Nykjaer A, Lee R, Teng KK, Jansen P, Madsen P, Nielsen MS, Jacobsen C, Kliemannel M, Schwarz E, Willnow TE, Hempstead BL, Petersen CM | title = Sortilin is essential for proNGF-induced neuronal cell death | journal = Nature | volume = 427 | issue = 6977 | pages = 843–8 | date = February 2004 | pmid = 14985763 | doi = 10.1038/nature02319}}</ref> Moreover, the function and role of sortilin is now emerging in several major human diseases such as [[atherosclerosis]] and [[coronary artery disease]], [[Alzheimer's disease|Alzheimer’s disease]], and [[cancer]].<ref name=pmid26950419>{{cite journal | vauthors = Goettsch C, Hutcheson JD, Aikawa M, Iwata H, Pham T, Nykjaer A, Kjolby M, Rogers M, Michel T, Shibasaki M, Hagita S, Kramann R, Rader DJ, Libby P, Singh SA, Aikawa E | title = Sortilin mediates vascular calcification via its recruitment into extracellular vesicles | journal = The Journal of Clinical Investigation | volume = 126 | issue = 4 | pages = 1323–36 | date = April 2016 | pmid = 26950419 | pmc = 4811143 | doi = 10.1172/JCI80851}}</ref><ref name="ReferenceB">{{cite journal | vauthors = Roselli S, Pundavela J, Demont Y, Faulkner S, Keene S, Attia J, Jiang CC, Zhang XD, Walker MM, Hondermarck H | title = Sortilin is associated with breast cancer aggressiveness and contributes to tumor cell adhesion and invasion | journal = Oncotarget | volume = 6 | issue = 12 | pages = 10473–86 | date = April 2015 | pmid = 25871389 | pmc = 4496368 | doi = 10.18632/oncotarget.3401}}</ref><ref name=pmid27066187>{{cite journal | vauthors = Wilson CM, Naves T, Al Akhrass H, Vincent F, Melloni B, Bonnaud F, Lalloué F, Jauberteau MO | title = A new role under sortilin's belt in cancer | journal = Communicative & Integrative Biology | volume = 9 | issue = 1 | pages = e1130192 | date = 2016-02-01 | pmid = 27066187 | pmc = 4802778 | doi = 10.1080/19420889.2015.1130192}}</ref> The ''SORT1'' gene also contains one of 27 [[Locus (genetics)|loci]] associated with increased risk of coronary artery disease.<ref name=pmid25748612>{{cite journal | vauthors = Mega JL, Stitziel NO, Smith JG, Chasman DI, Caulfield MJ, Devlin JJ, Nordio F, Hyde CL, Cannon CP, Sacks FM, Poulter NR, Sever PS, Ridker PM, Braunwald E, Melander O, Kathiresan S, Sabatine MS | title = Genetic risk, coronary heart disease events, and the clinical benefit of statin therapy: an analysis of primary and secondary prevention trials | journal = Lancet | volume = 385 | issue = 9984 | pages = 2264–71 | date = June 2015 | pmid = 25748612 | pmc = 4608367 | doi = 10.1016/S0140-6736(14)61730-X}}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Structure ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Sortilin 1
| HGNCid = 11186
| Symbol = SORT1
| AltSymbols =; NT3; Gp95
| OMIM = 602458
| ECnumber = 
| Homologene = 39282
| MGIid = 1338015
| GeneAtlas_image1 = PBB_GE_SORT1_212797_at_tn.png
| GeneAtlas_image2 = PBB_GE_SORT1_212807_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0016492 |text = neurotensin receptor activity, G-protein coupled}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030140 |text = trans-Golgi network transport vesicle}}
| Process = {{GNF_GO|id=GO:0001503 |text = ossification}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006897 |text = endocytosis}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6272
    | Hs_Ensembl = ENSG00000134243
    | Hs_RefseqProtein = NP_002950
    | Hs_RefseqmRNA = NM_002959
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 109653715
    | Hs_GenLoc_end = 109742096
    | Hs_Uniprot = Q99523
    | Mm_EntrezGene = 20661
    | Mm_Ensembl = ENSMUSG00000068747
    | Mm_RefseqmRNA = NM_019972
    | Mm_RefseqProtein = NP_064356
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 108412147
    | Mm_GenLoc_end = 108489567
    | Mm_Uniprot = Q6PHU5
  }}
}}
'''Sortilin 1''', also known as '''SORT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SORT1 sortilin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6272| accessdate = }}</ref>


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=== Gene ===
{{PBB_Summary
The ''SORT1'' gene resides on chromosome 1 at the band 1p13.3 and includes 23 [[exon]]s.<ref name="entrez" /> This gene encodes 2 [[isoforms]] through [[alternative splicing]].<ref>{{Cite web|url=http://www.uniprot.org/uniprot/Q99523|title=SORT1 - Sortilin precursor - Homo sapiens (Human) - SORT1 gene & protein|website=www.uniprot.org|access-date=2016-08-16}}</ref>
| section_title =  
| summary_text = This gene encodes a protein that is a multi-ligand type-1 receptor with similarity to the yeast carboxypeptidase Y sorting receptor Vps10 protein. The encoded protein, a trans-Golgi network (TGN) transmembrane protein, binds a number of unrelated ligands that participate in a wide range of cellular processes; however, it lacks the typical features of a signalling receptor. In the TGN, furin mediates the activation of the mature binding form. The encoded protein consists of a large luminal domain, a single transmembrane segment and short C-terminal cytoplasmic tail. The luminal domain contains a cysteine-rich region similar to two corresponding segments in the yeast Vps10p; the cytoplasmic tail is similar to the corresponding segment of the cation-independent mannose 6-phosphate receptor and the tail also interacts with the VHS domains of GGA (Golgi-associated, gamma-adaptin homologous, ARF-interacting) proteins.<ref name="entrez">{{cite web | title = Entrez Gene: SORT1 sortilin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6272| accessdate = }}</ref>
}}


==See also==
=== Protein ===
Sortilin is a member of the Vps10p sorting receptor family.<ref name="ReferenceA"/> [[Crystallization]] studies of the protein reveal that, when complexed with the [[ligand]] [[neurotensin]], the Vps10 [[ectodomain]] of sortilin forms a ten-bladed beta-propeller structure with an inner tunnel that contains multiple ligand [[binding site]]s.<ref>{{cite journal | vauthors = Quistgaard EM, Madsen P, Grøftehauge MK, Nissen P, Petersen CM, Thirup SS | title = Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller domain | journal = Nature Structural & Molecular Biology | volume = 16 | issue = 1 | pages = 96–8 | date = January 2009 | pmid = 19122660 | doi = 10.1038/nsmb.1543}}</ref> To prevent premature ligand binding during its [[Protein Synthesis|synthesis]], the [[Protein precursor|precursor protein]] of sortilin contains a 44-[[amino acid]] [[Propeptide|pro-peptide]] that serves as a [[Chaperone (protein)|chaperone]] for the Vps10p domain.<ref name=pmid22341525>{{cite journal | vauthors = Nykjaer A, Willnow TE | title = Sortilin: a receptor to regulate neuronal viability and function | journal = Trends in Neurosciences | volume = 35 | issue = 4 | pages = 261–70 | date = April 2012 | pmid = 22341525 | doi = 10.1016/j.tins.2012.01.003}}</ref> In addition, two [[Hydrophobic effect|hydrophobic loops]] have been detected in this domain and act to anchor the protein in the cell membrane.<ref>{{cite journal | vauthors = Quistgaard EM, Grøftehauge MK, Madsen P, Pallesen LT, Christensen B, Sørensen ES, Nissen P, Petersen CM, Thirup SS | title = Revisiting the structure of the Vps10 domain of human sortilin and its interaction with neurotensin | journal = Protein Science | volume = 23 | issue = 9 | pages = 1291–300 | date = September 2014 | pmid = 24985322 | pmc = 4243999 | doi = 10.1002/pro.2512}}</ref>
 
== Function ==
 
In humans, sortilin is expressed over a wide range of cell types and tissues such as the [[brain]], [[spinal cord]], [[adrenal gland]], [[thyroid]], [[B-lymphocytes]], [[adipocyte]]s, [[skeletal muscle]], and [[heart]].<ref>{{cite journal | vauthors = Schmidt V, Willnow TE | title = Protein sorting gone wrong--VPS10P domain receptors in cardiovascular and metabolic diseases | journal = Atherosclerosis | volume = 245 | pages = 194–9 | date = February 2016 | pmid = 26724530 | doi = 10.1016/j.atherosclerosis.2015.11.027}}</ref> As a sorting receptor on the [[cell surface]] and on the [[endoplasmic reticulum]]-Golgi apparatus within the cell, sortilin is involved in the [[Protein transport|transport]] of a wide variety of intracellular proteins between the trans-Golgi network, endosome, lysosome, and [[secretory granule]]s, as well as the plasma membrane.<ref name=pmid11331584/> This molecular function enables sortilin to participate in various biological processes, including the transport of [[GLUT4]] to the plasma membrane of [[Fat cells|fat]] and [[skeletal muscle cells]] in response to [[insulin]].<ref name=pmid23966466/> It also mediates the interaction between [[NGF (gene)|proNGF]] and the [[p75NTR]]:sortilin [[Protein complexes|complex]] by acting as a [[co-receptor]] to signal cell death.<ref name=pmid14985763/><ref name=pmid22341525/> The fine regulation of the [[brain-derived neurotrophic factor]] (BDNF) by sortilin is required for both neuronal and [[tumor cell]] survival.<ref>{{cite journal | vauthors = Akil H, Perraud A, Mélin C, Jauberteau MO, Mathonnet M | title = Fine-tuning roles of endogenous brain-derived neurotrophic factor, TrkB and sortilin in colorectal cancer cell survival | journal = PLoS One | volume = 6 | issue = 9 | pages = e25097 | date = 2011-01-01 | pmid = 21966426 | pmc = 3180371 | doi = 10.1371/journal.pone.0025097}}</ref> Moreover, sortilin has been implicated in [[Low-density lipoprotein|LDL]]-[[cholesterol]] metabolism, [[Very low-density lipoprotein|VLDL]] secretion, and [[PCSK9]] secretion, and thus plays a role in the development of atherosclerotic [[lesion]]s.<ref name=pmid25593281/><ref name=pmid25702058/> Other processes involving sortilin include [[endocytosis]],<ref name=pmid11331584/> negative regulation of [[lipoprotein]] [[lipase]] activity,<ref>{{cite journal | vauthors = Nielsen MS, Jacobsen C, Olivecrona G, Gliemann J, Petersen CM | title = Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase | journal = The Journal of Biological Chemistry | volume = 274 | issue = 13 | pages = 8832–6 | date = March 1999 | pmid = 10085125 | doi=10.1074/jbc.274.13.8832}}</ref> [[myotube]] [[Differentiation (biology)|differentiation]],<ref name="ReferenceC">{{cite journal | vauthors = Ariga M, Nedachi T, Katagiri H, Kanzaki M | title = Functional role of sortilin in myogenesis and development of insulin-responsive glucose transport system in C2C12 myocytes | journal = The Journal of Biological Chemistry | volume = 283 | issue = 15 | pages = 10208–20 | date = April 2008 | pmid = 18258592 | doi = 10.1074/jbc.M710604200}}</ref> [[ossification]],<ref>{{cite journal | vauthors = Maeda S, Nobukuni T, Shimo-Onoda K, Hayashi K, Yone K, Komiya S, Inoue I | title = Sortilin is upregulated during osteoblastic differentiation of mesenchymal stem cells and promotes extracellular matrix mineralization | journal = Journal of Cellular Physiology | volume = 193 | issue = 1 | pages = 73–9 | date = October 2002 | pmid = 12209882 | doi = 10.1002/jcp.10151}}</ref> and regulation of [[gene expression]].<ref name="ReferenceC"/>
 
== Clinical significance ==
Given its function in facilitating [[Protein degradation|lysosomal degradation]] or recycling of ligands in lipid metabolism<ref name=pmid25702058/><ref name=pmid26950419/><ref>{{cite journal | vauthors = Strong A, Rader DJ | title = Sortilin as a regulator of lipoprotein metabolism | journal = Current Atherosclerosis Reports | volume = 14 | issue = 3 | pages = 211–8 | date = June 2012 | pmid = 22538429 | doi = 10.1007/s11883-012-0248-x}}</ref><ref>{{cite journal | vauthors = Zhong LY, Cayabyab FS, Tang CK, Zheng XL, Peng TH, Lv YC | title = Sortilin: A novel regulator in lipid metabolism and atherogenesis | journal = Clinica Chimica Acta | volume = 460 | pages = 11–7 | date = September 2016 | pmid = 27312323 | doi = 10.1016/j.cca.2016.06.013}}</ref><ref>{{cite journal | vauthors = Kjolby M, Andersen OM, Breiderhoff T, Fjorback AW, Pedersen KM, Madsen P, Jansen P, Heeren J, Willnow TE, Nykjaer A | title = Sort1, encoded by the cardiovascular risk locus 1p13.3, is a regulator of hepatic lipoprotein export | journal = Cell Metabolism | volume = 12 | issue = 3 | pages = 213–23 | date = September 2010 | pmid = 20816088 | doi = 10.1016/j.cmet.2010.08.006}}</ref> and the neural system,<ref name=pmid24121631>{{cite journal | vauthors = Carlo AS | title = Sortilin, a novel APOE receptor implicated in Alzheimer disease | journal = Prion | volume = 7 | issue = 5 | pages = 378–82 | date = 2013-10-01 | pmid = 24121631 | pmc = 4134342 | doi = 10.4161/pri.26746}}</ref> sortilin likely plays an important role in the underlying mechanisms and [[pathophysiology]] of atherogenesis and coronary artery disease, as well as in [[neurological disorder]]s. For example, sortilin has been identified as an important receptor for brain [[apolipoprotein E]] (APOE) metabolism, which is implicated in the underlying mechanisms of Alzheimer’s disease.<ref name=pmid24121631/><ref>{{cite journal | vauthors = Jin C, Liu X, Zhang F, Wu Y, Yuan J, Zhu J, Zhang F, Wang G, Cheng Z | title = An updated meta-analysis of the association between SORL1 variants and the risk for sporadic Alzheimer's disease | journal = Journal of Alzheimer's Disease | volume = 37 | issue = 2 | pages = 429–37 | date = 2013-01-01 | pmid = 23948893 | doi = 10.3233/JAD-130533}}</ref><ref>{{cite journal | vauthors = Piscopo P, Tosto G, Belli C, Talarico G, Galimberti D, Gasparini M, Canevelli M, Poleggi A, Crestini A, Albani D, Forloni G, Lucca U, Quadri P, Tettamanti M, Fenoglio C, Scarpini E, Bruno G, Vanacore N, Confaloni A | title = SORL1 Gene is Associated with the Conversion from Mild Cognitive Impairment to Alzheimer's Disease | journal = Journal of Alzheimer's Disease | volume = 46 | issue = 3 | pages = 771–6 | date = 2015-01-01 | pmid = 25881907 | doi = 10.3233/JAD-141551}}</ref><ref>{{cite journal | vauthors = Andersson CH, Hansson O, Minthon L, Andreasen N, Blennow K, Zetterberg H, Skoog I, Wallin A, Nilsson S, Kettunen P | title = A Genetic Variant of the Sortilin 1 Gene is Associated with Reduced Risk of Alzheimer's Disease | journal = Journal of Alzheimer's Disease | date = July 2016 | pmid = 27392867 | doi = 10.3233/JAD-160319 | volume=53 | pages=1353–63}}</ref> Interestingly, a significant role for sortilin has recently also been reported in the field of [[oncology]], as it has been detected in several [[cancer cell lines]]. Notably, human cancerous [[epithelial cells]] exhibited increased levels of sortilin as compared to normal epithelial tissues. Furthermore, it appears that sortilin participates in the progression of [[breast cancer]] and contributes to tumor [[cell adhesion]] and invasion.<ref name="ReferenceB"/><ref name=pmid27066187/>
 
=== Clinical marker ===
In 2007, chromosome 1p13.3 was identified as a promising locus through a [[Genome-wide association study|genome-wide]] approach in patients with coronary artery disease.<ref name=pmid17634449>{{cite journal | vauthors = Samani NJ, Erdmann J, Hall AS, Hengstenberg C, Mangino M, Mayer B, Dixon RJ, Meitinger T, Braund P, Wichmann HE, Barrett JH, König IR, Stevens SE, Szymczak S, Tregouet DA, Iles MM, Pahlke F, Pollard H, Lieb W, Cambien F, Fischer M, Ouwehand W, Blankenberg S, Balmforth AJ, Baessler A, Ball SG, Strom TM, Braenne I, Gieger C, Deloukas P, Tobin MD, Ziegler A, Thompson JR, Schunkert H | title = Genomewide association analysis of coronary artery disease | journal = The New England Journal of Medicine | volume = 357 | issue = 5 | pages = 443–53 | date = August 2007 | pmid = 17634449 | pmc = 2719290 | doi = 10.1056/NEJMoa072366}}</ref> Subsequently, accumulating evidence suggests that the ''SORT1'' gene at the 1p13 locus is an important risk factor for coronary artery disease, which is attributed to [[lipid metabolism disorder]]s.<ref name=pmid17634449/><ref>{{cite journal | vauthors = Nikpay M, Goel A, Won HH, Hall LM, Willenborg C, Kanoni S, Saleheen D, Kyriakou T, Nelson CP, Hopewell JC, Webb TR, Zeng L, Dehghan A, Alver M, Armasu SM, Auro K, Bjonnes A, Chasman DI, Chen S, Ford I, Franceschini N, Gieger C, Grace C, Gustafsson S, Huang J, Hwang SJ, Kim YK, Kleber ME, Lau KW, Lu X, Lu Y, Lyytikäinen LP, Mihailov E, Morrison AC, Pervjakova N, Qu L, Rose LM, Salfati E, Saxena R, Scholz M, Smith AV, Tikkanen E, Uitterlinden A, Yang X, Zhang W, Zhao W, de Andrade M, de Vries PS, van Zuydam NR, Anand SS, Bertram L, Beutner F, Dedoussis G, Frossard P, Gauguier D, Goodall AH, Gottesman O, Haber M, Han BG, Huang J, Jalilzadeh S, Kessler T, König IR, Lannfelt L, Lieb W, Lind L, Lindgren CM, Lokki ML, Magnusson PK, Mallick NH, Mehra N, Meitinger T, Memon FU, Morris AP, Nieminen MS, Pedersen NL, Peters A, Rallidis LS, Rasheed A, Samuel M, Shah SH, Sinisalo J, Stirrups KE, Trompet S, Wang L, Zaman KS, Ardissino D, Boerwinkle E, Borecki IB, Bottinger EP, Buring JE, Chambers JC, Collins R, Cupples LA, Danesh J, Demuth I, Elosua R, Epstein SE, Esko T, Feitosa MF, Franco OH, Franzosi MG, Granger CB, Gu D, Gudnason V, Hall AS, Hamsten A, Harris TB, Hazen SL, Hengstenberg C, Hofman A, Ingelsson E, Iribarren C, Jukema JW, Karhunen PJ, Kim BJ, Kooner JS, Kullo IJ, Lehtimäki T, Loos RJ, Melander O, Metspalu A, März W, Palmer CN, Perola M, Quertermous T, Rader DJ, Ridker PM, Ripatti S, Roberts R, Salomaa V, Sanghera DK, Schwartz SM, Seedorf U, Stewart AF, Stott DJ, Thiery J, Zalloua PA, O'Donnell CJ, Reilly MP, Assimes TL, Thompson JR, Erdmann J, Clarke R, Watkins H, Kathiresan S, McPherson R, Deloukas P, Schunkert H, Samani NJ, Farrall M | display-authors = 6 | title = A comprehensive 1,000 Genomes-based genome-wide association meta-analysis of coronary artery disease | journal = Nature Genetics | volume = 47 | issue = 10 | pages = 1121–30 | date = October 2015 | pmid = 26343387 | pmc = 4589895 | doi = 10.1038/ng.3396}}</ref><ref>{{cite journal | vauthors = Zeller T, Blankenberg S, Diemert P | title = Genomewide association studies in cardiovascular disease--an update 2011 | journal = Clinical Chemistry | volume = 58 | issue = 1 | pages = 92–103 | date = January 2012 | pmid = 22125304 | doi = 10.1373/clinchem.2011.170431}}</ref> As the role of sortilin in lipid metabolism and the development of atherosclerosis has been established, a recent study further reported that increased release of soluble sortilin from platelets, measured as circulating sortilin, may be associated with in vivo platelet activation.<ref name=pmid27085161>{{cite journal | vauthors = Ogawa K, Ueno T, Iwasaki T, Kujiraoka T, Ishihara M, Kunimoto S, Takayama T, Kanai T, Hirayama A, Hattori H | title = Soluble sortilin is released by activated platelets and its circulating levels are associated with cardiovascular risk factors | journal = Atherosclerosis | volume = 249 | pages = 110–5 | date = June 2016 | pmid = 27085161 | doi = 10.1016/j.atherosclerosis.2016.03.041}}</ref> This observation also indicates that sortilin has a potential application as a clinical biomarker for diagnosis and prognosis.<ref name=pmid25593281/><ref name=pmid27085161/> Additionally, a multi-locus genetic risk score study, based on a combination of 27 loci including the ''SORT1'' gene, identified individuals at increased risk for both incident and recurrent coronary artery disease events, as well as an enhanced clinical benefit from [[statin]] therapy. The study was based on a community [[cohort study]] (the Malmo Diet and Cancer study) and four additional [[randomized controlled trial]]s of primary prevention cohorts (JUPITER and ASCOT) and secondary prevention cohorts (CARE and PROVE IT-TIMI 22).<ref name=pmid25748612/>
 
== Interactions ==
 
Sortilin has been shown to [[Protein-protein interaction|interact]] with [[GGA1]]<ref name=pmid11821067>{{cite journal | vauthors = Jacobsen L, Madsen P, Nielsen MS, Geraerts WP, Gliemann J, Smit AB, Petersen CM | title = The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding | journal = FEBS Letters | volume = 511 | issue = 1-3 | pages = 155–8 | date = January 2002 | pmid = 11821067 | doi = 10.1016/S0014-5793(01)03299-9 }}</ref> and [[GGA2]].<ref name=pmid11331584/><ref name=pmid11821067/>
 
=== Interactive Pathway Map ===
Sortilin participates in interactions within the [http://www.wikipathways.org/index.php/Pathway:WP3578 trans-Golgi network vesicle budding] and [http://www.wikipathways.org/index.php/Pathway:WP2380 BDNF signaling pathways].
 
== See also ==
* [[Neurotensin receptor]]
* [[Neurotensin receptor]]


==References==
== References ==
{{reflist|2}}
{{reflist|33em}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin|33em}}
{{PBB_Further_reading
* {{cite journal | vauthors = Vincent JP, Mazella J, Kitabgi P | title = Neurotensin and neurotensin receptors | journal = Trends in Pharmacological Sciences | volume = 20 | issue = 7 | pages = 302–9 | date = July 1999 | pmid = 10390649 | doi = 10.1016/S0165-6147(99)01357-7 }}
| citations =
* {{cite journal | vauthors = Mazella J | title = Sortilin/neurotensin receptor-3: a new tool to investigate neurotensin signaling and cellular trafficking? | journal = Cellular Signalling | volume = 13 | issue = 1 | pages = 1–6 | date = January 2001 | pmid = 11257441 | doi = 10.1016/S0898-6568(00)00130-3 }}
*{{cite journal | author=Vincent JP, Mazella J, Kitabgi P |title=Neurotensin and neurotensin receptors. |journal=Trends Pharmacol. Sci. |volume=20 |issue= 7 |pages= 302-9 |year= 1999 |pmid= 10390649 |doi= }}
* {{cite journal | vauthors = Petersen CM, Nielsen MS, Nykjaer A, Jacobsen L, Tommerup N, Rasmussen HH, Roigaard H, Gliemann J, Madsen P, Moestrup SK | title = Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography | journal = The Journal of Biological Chemistry | volume = 272 | issue = 6 | pages = 3599–605 | date = February 1997 | pmid = 9013611 | doi = 10.1074/jbc.272.6.3599 }}
*{{cite journal | author=Mazella J |title=Sortilin/neurotensin receptor-3: a new tool to investigate neurotensin signaling and cellular trafficking? |journal=Cell. Signal. |volume=13 |issue= 1 |pages= 1-6 |year= 2001 |pmid= 11257441 |doi= }}
* {{cite journal | vauthors = Lin BZ, Pilch PF, Kandror KV | title = Sortilin is a major protein component of Glut4-containing vesicles | journal = The Journal of Biological Chemistry | volume = 272 | issue = 39 | pages = 24145–7 | date = September 1997 | pmid = 9305862 | doi = 10.1074/jbc.272.39.24145 }}
*{{cite journal | author=Petersen CM, Nielsen MS, Nykjaer A, ''et al.'' |title=Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography. |journal=J. Biol. Chem. |volume=272 |issue= 6 |pages= 3599-605 |year= 1997 |pmid= 9013611 |doi= }}
* {{cite journal | vauthors = Tauris J, Ellgaard L, Jacobsen C, Nielsen MS, Madsen P, Thøgersen HC, Gliemann J, Petersen CM, Moestrup SK | title = The carboxy-terminal domain of the receptor-associated protein binds to the Vps10p domain of sortilin | journal = FEBS Letters | volume = 429 | issue = 1 | pages = 27–30 | date = June 1998 | pmid = 9657377 | doi = 10.1016/S0014-5793(98)00559-6 }}
*{{cite journal | author=Lin BZ, Pilch PF, Kandror KV |title=Sortilin is a major protein component of Glut4-containing vesicles. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24145-7 |year= 1997 |pmid= 9305862 |doi= }}
* {{cite journal | vauthors = Mazella J, Zsürger N, Navarro V, Chabry J, Kaghad M, Caput D, Ferrara P, Vita N, Gully D, Maffrand JP, Vincent JP | title = The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor | journal = The Journal of Biological Chemistry | volume = 273 | issue = 41 | pages = 26273–6 | date = October 1998 | pmid = 9756851 | doi = 10.1074/jbc.273.41.26273 }}
*{{cite journal | author=Tauris J, Ellgaard L, Jacobsen C, ''et al.'' |title=The carboxy-terminal domain of the receptor-associated protein binds to the Vps10p domain of sortilin. |journal=FEBS Lett. |volume=429 |issue= 1 |pages= 27-30 |year= 1998 |pmid= 9657377 |doi= }}
* {{cite journal | vauthors = Munck Petersen C, Nielsen MS, Jacobsen C, Tauris J, Jacobsen L, Gliemann J, Moestrup SK, Madsen P | title = Propeptide cleavage conditions sortilin/neurotensin receptor-3 for ligand binding | journal = The EMBO Journal | volume = 18 | issue = 3 | pages = 595–604 | date = February 1999 | pmid = 9927419 | pmc = 1171152 | doi = 10.1093/emboj/18.3.595 }}
*{{cite journal | author=Mazella J, Zsürger N, Navarro V, ''et al.'' |title=The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor. |journal=J. Biol. Chem. |volume=273 |issue= 41 |pages= 26273-6 |year= 1998 |pmid= 9756851 |doi= }}
* {{cite journal | vauthors = Nielsen MS, Jacobsen C, Olivecrona G, Gliemann J, Petersen CM | title = Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase | journal = The Journal of Biological Chemistry | volume = 274 | issue = 13 | pages = 8832–6 | date = March 1999 | pmid = 10085125 | doi = 10.1074/jbc.274.13.8832 }}
*{{cite journal | author=Munck Petersen C, Nielsen MS, Jacobsen C, ''et al.'' |title=Propeptide cleavage conditions sortilin/neurotensin receptor-3 for ligand binding. |journal=EMBO J. |volume=18 |issue= 3 |pages= 595-604 |year= 1999 |pmid= 9927419 |doi= 10.1093/emboj/18.3.595 }}
* {{cite journal | vauthors = Nielsen MS, Madsen P, Christensen EI, Nykjaer A, Gliemann J, Kasper D, Pohlmann R, Petersen CM | title = The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein | journal = The EMBO Journal | volume = 20 | issue = 9 | pages = 2180–90 | date = May 2001 | pmid = 11331584 | pmc = 125444 | doi = 10.1093/emboj/20.9.2180 }}
*{{cite journal | author=Nielsen MS, Jacobsen C, Olivecrona G, ''et al.'' |title=Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. |journal=J. Biol. Chem. |volume=274 |issue= 13 |pages= 8832-6 |year= 1999 |pmid= 10085125 |doi= }}
* {{cite journal | vauthors = Takatsu H, Katoh Y, Shiba Y, Nakayama K | title = Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains | journal = The Journal of Biological Chemistry | volume = 276 | issue = 30 | pages = 28541–5 | date = July 2001 | pmid = 11390366 | doi = 10.1074/jbc.C100218200 }}
*{{cite journal | author=Nielsen MS, Madsen P, Christensen EI, ''et al.'' |title=The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein. |journal=EMBO J. |volume=20 |issue= 9 |pages= 2180-90 |year= 2001 |pmid= 11331584 |doi= 10.1093/emboj/20.9.2180 }}
* {{cite journal | vauthors = Hampe W, Rezgaoui M, Hermans-Borgmeyer I, Schaller HC | title = The genes for the human VPS10 domain-containing receptors are large and contain many small exons | journal = Human Genetics | volume = 108 | issue = 6 | pages = 529–36 | date = June 2001 | pmid = 11499680 | doi = 10.1007/s004390100504 }}
*{{cite journal | author=Takatsu H, Katoh Y, Shiba Y, Nakayama K |title=Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 28541-5 |year= 2001 |pmid= 11390366 |doi= 10.1074/jbc.C100218200 }}
* {{cite journal | vauthors = Shiba T, Takatsu H, Nogi T, Matsugaki N, Kawasaki M, Igarashi N, Suzuki M, Kato R, Earnest T, Nakayama K, Wakatsuki S | title = Structural basis for recognition of acidic-cluster dileucine sequence by GGA1 | journal = Nature | volume = 415 | issue = 6874 | pages = 937–41 | date = February 2002 | pmid = 11859376 | doi = 10.1038/415937a }}
*{{cite journal | author=Hampe W, Rezgaoui M, Hermans-Borgmeyer I, Schaller HC |title=The genes for the human VPS10 domain-containing receptors are large and contain many small exons. |journal=Hum. Genet. |volume=108 |issue= 6 |pages= 529-36 |year= 2001 |pmid= 11499680 |doi= }}
* {{cite journal | vauthors = Maeda S, Nobukuni T, Shimo-Onoda K, Hayashi K, Yone K, Komiya S, Inoue I | title = Sortilin is upregulated during osteoblastic differentiation of mesenchymal stem cells and promotes extracellular matrix mineralization | journal = Journal of Cellular Physiology | volume = 193 | issue = 1 | pages = 73–9 | date = October 2002 | pmid = 12209882 | doi = 10.1002/jcp.10151 }}
*{{cite journal | author=Shiba T, Takatsu H, Nogi T, ''et al.'' |title=Structural basis for recognition of acidic-cluster dileucine sequence by GGA1. |journal=Nature |volume=415 |issue= 6874 |pages= 937-41 |year= 2002 |pmid= 11859376 |doi= 10.1038/415937a }}
* {{cite journal | vauthors = Martin S, Navarro V, Vincent JP, Mazella J | title = Neurotensin receptor-1 and -3 complex modulates the cellular signaling of neurotensin in the HT29 cell line | journal = Gastroenterology | volume = 123 | issue = 4 | pages = 1135–43 | date = October 2002 | pmid = 12360476 | doi = 10.1053/gast.2002.36000 }}
*{{cite journal | author=Maeda S, Nobukuni T, Shimo-Onoda K, ''et al.'' |title=Sortilin is upregulated during osteoblastic differentiation of mesenchymal stem cells and promotes extracellular matrix mineralization. |journal=J. Cell. Physiol. |volume=193 |issue= 1 |pages= 73-9 |year= 2002 |pmid= 12209882 |doi= 10.1002/jcp.10151 }}
* {{cite journal | vauthors = Navarro V, Vincent JP, Mazella J | title = Shedding of the luminal domain of the neurotensin receptor-3/sortilin in the HT29 cell line | journal = Biochemical and Biophysical Research Communications | volume = 298 | issue = 5 | pages = 760–4 | date = November 2002 | pmid = 12419319 | doi = 10.1016/S0006-291X(02)02564-0 }}
*{{cite journal | author=Martin S, Navarro V, Vincent JP, Mazella J |title=Neurotensin receptor-1 and -3 complex modulates the cellular signaling of neurotensin in the HT29 cell line. |journal=Gastroenterology |volume=123 |issue= 4 |pages= 1135-43 |year= 2002 |pmid= 12360476 |doi= }}
* {{cite journal | vauthors = Martin S, Vincent JP, Mazella J | title = Involvement of the neurotensin receptor-3 in the neurotensin-induced migration of human microglia | journal = The Journal of Neuroscience | volume = 23 | issue = 4 | pages = 1198–205 | date = February 2003 | pmid = 12598608 | doi =  }}
*{{cite journal | author=Navarro V, Vincent JP, Mazella J |title=Shedding of the luminal domain of the neurotensin receptor-3/sortilin in the HT29 cell line. |journal=Biochem. Biophys. Res. Commun. |volume=298 |issue= 5 |pages= 760-4 |year= 2003 |pmid= 12419319 |doi= }}
* {{cite journal | vauthors = Lefrancois S, Zeng J, Hassan AJ, Canuel M, Morales CR | title = The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin | journal = The EMBO Journal | volume = 22 | issue = 24 | pages = 6430–7 | date = December 2003 | pmid = 14657016 | pmc = 291824 | doi = 10.1093/emboj/cdg629 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Martin S, Vincent JP, Mazella J |title=Involvement of the neurotensin receptor-3 in the neurotensin-induced migration of human microglia. |journal=J. Neurosci. |volume=23 |issue= 4 |pages= 1198-205 |year= 2003 |pmid= 12598608 |doi=  }}
*{{cite journal | author=Lefrancois S, Zeng J, Hassan AJ, ''et al.'' |title=The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6430-7 |year= 2004 |pmid= 14657016 |doi= 10.1093/emboj/cdg629 }}
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Revision as of 02:07, 25 October 2017

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Sortilin (SORT1) is a protein that in humans is encoded by the SORT1 gene on chromosome 1.[1] This protein is a type I membrane glycoprotein in the vacuolar protein sorting 10 protein (Vps10p) family of sorting receptors. While it is ubiquitously expressed in many tissues,[2] sortilin is most abundant in the central nervous system.[3] At the cellular level, sortilin functions in protein transport between the Golgi apparatus, endosome, lysosome, and plasma membrane, leading to its involvement in multiple biological processes such as glucose and lipid metabolism as well as neural development and cell death.[4][5][6][7][8] Moreover, the function and role of sortilin is now emerging in several major human diseases such as atherosclerosis and coronary artery disease, Alzheimer’s disease, and cancer.[9][10][11] The SORT1 gene also contains one of 27 loci associated with increased risk of coronary artery disease.[12]

Structure

Gene

The SORT1 gene resides on chromosome 1 at the band 1p13.3 and includes 23 exons.[1] This gene encodes 2 isoforms through alternative splicing.[13]

Protein

Sortilin is a member of the Vps10p sorting receptor family.[3] Crystallization studies of the protein reveal that, when complexed with the ligand neurotensin, the Vps10 ectodomain of sortilin forms a ten-bladed beta-propeller structure with an inner tunnel that contains multiple ligand binding sites.[14] To prevent premature ligand binding during its synthesis, the precursor protein of sortilin contains a 44-amino acid pro-peptide that serves as a chaperone for the Vps10p domain.[15] In addition, two hydrophobic loops have been detected in this domain and act to anchor the protein in the cell membrane.[16]

Function

In humans, sortilin is expressed over a wide range of cell types and tissues such as the brain, spinal cord, adrenal gland, thyroid, B-lymphocytes, adipocytes, skeletal muscle, and heart.[17] As a sorting receptor on the cell surface and on the endoplasmic reticulum-Golgi apparatus within the cell, sortilin is involved in the transport of a wide variety of intracellular proteins between the trans-Golgi network, endosome, lysosome, and secretory granules, as well as the plasma membrane.[4] This molecular function enables sortilin to participate in various biological processes, including the transport of GLUT4 to the plasma membrane of fat and skeletal muscle cells in response to insulin.[5] It also mediates the interaction between proNGF and the p75NTR:sortilin complex by acting as a co-receptor to signal cell death.[8][15] The fine regulation of the brain-derived neurotrophic factor (BDNF) by sortilin is required for both neuronal and tumor cell survival.[18] Moreover, sortilin has been implicated in LDL-cholesterol metabolism, VLDL secretion, and PCSK9 secretion, and thus plays a role in the development of atherosclerotic lesions.[6][7] Other processes involving sortilin include endocytosis,[4] negative regulation of lipoprotein lipase activity,[19] myotube differentiation,[20] ossification,[21] and regulation of gene expression.[20]

Clinical significance

Given its function in facilitating lysosomal degradation or recycling of ligands in lipid metabolism[7][9][22][23][24] and the neural system,[25] sortilin likely plays an important role in the underlying mechanisms and pathophysiology of atherogenesis and coronary artery disease, as well as in neurological disorders. For example, sortilin has been identified as an important receptor for brain apolipoprotein E (APOE) metabolism, which is implicated in the underlying mechanisms of Alzheimer’s disease.[25][26][27][28] Interestingly, a significant role for sortilin has recently also been reported in the field of oncology, as it has been detected in several cancer cell lines. Notably, human cancerous epithelial cells exhibited increased levels of sortilin as compared to normal epithelial tissues. Furthermore, it appears that sortilin participates in the progression of breast cancer and contributes to tumor cell adhesion and invasion.[10][11]

Clinical marker

In 2007, chromosome 1p13.3 was identified as a promising locus through a genome-wide approach in patients with coronary artery disease.[29] Subsequently, accumulating evidence suggests that the SORT1 gene at the 1p13 locus is an important risk factor for coronary artery disease, which is attributed to lipid metabolism disorders.[29][30][31] As the role of sortilin in lipid metabolism and the development of atherosclerosis has been established, a recent study further reported that increased release of soluble sortilin from platelets, measured as circulating sortilin, may be associated with in vivo platelet activation.[32] This observation also indicates that sortilin has a potential application as a clinical biomarker for diagnosis and prognosis.[6][32] Additionally, a multi-locus genetic risk score study, based on a combination of 27 loci including the SORT1 gene, identified individuals at increased risk for both incident and recurrent coronary artery disease events, as well as an enhanced clinical benefit from statin therapy. The study was based on a community cohort study (the Malmo Diet and Cancer study) and four additional randomized controlled trials of primary prevention cohorts (JUPITER and ASCOT) and secondary prevention cohorts (CARE and PROVE IT-TIMI 22).[12]

Interactions

Sortilin has been shown to interact with GGA1[33] and GGA2.[4][33]

Interactive Pathway Map

Sortilin participates in interactions within the trans-Golgi network vesicle budding and BDNF signaling pathways.

See also

References

  1. ↑ 1.0 1.1 "Entrez Gene: SORT1 sortilin 1".
  2. ↑ "BioGPS - your Gene Portal System". biogps.org. Retrieved 2016-08-16.
  3. ↑ 3.0 3.1 Andersen JL, Schrøder TJ, Christensen S, Strandbygård D, Pallesen LT, García-Alai MM, Lindberg S, Langgård M, Eskildsen JC, David L, Tagmose L, Simonsen KB, Maltas PJ, Rønn LC, de Jong IE, Malik IJ, Egebjerg J, Karlsson JJ, Uppalanchi S, Sakumudi DR, Eradi P, Watson SP, Thirup S (February 2014). "Identification of the first small-molecule ligand of the neuronal receptor sortilin and structure determination of the receptor-ligand complex". Acta Crystallographica Section D. 70 (Pt 2): 451–60. doi:10.1107/S1399004713030149. PMC 3940197. PMID 24531479.
  4. ↑ 4.0 4.1 4.2 4.3 Nielsen MS, Madsen P, Christensen EI, Nykjaer A, Gliemann J, Kasper D, Pohlmann R, Petersen CM (May 2001). "The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein". The EMBO Journal. 20 (9): 2180–90. doi:10.1093/emboj/20.9.2180. PMC 125444. PMID 11331584.
  5. ↑ 5.0 5.1 Huang G, Buckler-Pena D, Nauta T, Singh M, Asmar A, Shi J, Kim JY, Kandror KV (October 2013). "Insulin responsiveness of glucose transporter 4 in 3T3-L1 cells depends on the presence of sortilin". Molecular Biology of the Cell. 24 (19): 3115–22. doi:10.1091/mbc.E12-10-0765. PMC 3784384. PMID 23966466.
  6. ↑ 6.0 6.1 6.2 Patel KM, Strong A, Tohyama J, Jin X, Morales CR, Billheimer J, Millar J, Kruth H, Rader DJ (February 2015). "Macrophage sortilin promotes LDL uptake, foam cell formation, and atherosclerosis". Circulation Research. 116 (5): 789–96. doi:10.1161/CIRCRESAHA.116.305811. PMC 4602371. PMID 25593281.
  7. ↑ 7.0 7.1 7.2 Kjolby M, Nielsen MS, Petersen CM (April 2015). "Sortilin, encoded by the cardiovascular risk gene SORT1, and its suggested functions in cardiovascular disease". Current Atherosclerosis Reports. 17 (4): 496. doi:10.1007/s11883-015-0496-7. PMID 25702058.
  8. ↑ 8.0 8.1 Nykjaer A, Lee R, Teng KK, Jansen P, Madsen P, Nielsen MS, Jacobsen C, Kliemannel M, Schwarz E, Willnow TE, Hempstead BL, Petersen CM (February 2004). "Sortilin is essential for proNGF-induced neuronal cell death". Nature. 427 (6977): 843–8. doi:10.1038/nature02319. PMID 14985763.
  9. ↑ 9.0 9.1 Goettsch C, Hutcheson JD, Aikawa M, Iwata H, Pham T, Nykjaer A, Kjolby M, Rogers M, Michel T, Shibasaki M, Hagita S, Kramann R, Rader DJ, Libby P, Singh SA, Aikawa E (April 2016). "Sortilin mediates vascular calcification via its recruitment into extracellular vesicles". The Journal of Clinical Investigation. 126 (4): 1323–36. doi:10.1172/JCI80851. PMC 4811143. PMID 26950419.
  10. ↑ 10.0 10.1 Roselli S, Pundavela J, Demont Y, Faulkner S, Keene S, Attia J, Jiang CC, Zhang XD, Walker MM, Hondermarck H (April 2015). "Sortilin is associated with breast cancer aggressiveness and contributes to tumor cell adhesion and invasion". Oncotarget. 6 (12): 10473–86. doi:10.18632/oncotarget.3401. PMC 4496368. PMID 25871389.
  11. ↑ 11.0 11.1 Wilson CM, Naves T, Al Akhrass H, Vincent F, Melloni B, Bonnaud F, Lalloué F, Jauberteau MO (2016-02-01). "A new role under sortilin's belt in cancer". Communicative & Integrative Biology. 9 (1): e1130192. doi:10.1080/19420889.2015.1130192. PMC 4802778. PMID 27066187.
  12. ↑ 12.0 12.1 Mega JL, Stitziel NO, Smith JG, Chasman DI, Caulfield MJ, Devlin JJ, Nordio F, Hyde CL, Cannon CP, Sacks FM, Poulter NR, Sever PS, Ridker PM, Braunwald E, Melander O, Kathiresan S, Sabatine MS (June 2015). "Genetic risk, coronary heart disease events, and the clinical benefit of statin therapy: an analysis of primary and secondary prevention trials". Lancet. 385 (9984): 2264–71. doi:10.1016/S0140-6736(14)61730-X. PMC 4608367. PMID 25748612.
  13. ↑ "SORT1 - Sortilin precursor - Homo sapiens (Human) - SORT1 gene & protein". www.uniprot.org. Retrieved 2016-08-16.
  14. ↑ Quistgaard EM, Madsen P, Grøftehauge MK, Nissen P, Petersen CM, Thirup SS (January 2009). "Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller domain". Nature Structural & Molecular Biology. 16 (1): 96–8. doi:10.1038/nsmb.1543. PMID 19122660.
  15. ↑ 15.0 15.1 Nykjaer A, Willnow TE (April 2012). "Sortilin: a receptor to regulate neuronal viability and function". Trends in Neurosciences. 35 (4): 261–70. doi:10.1016/j.tins.2012.01.003. PMID 22341525.
  16. ↑ Quistgaard EM, Grøftehauge MK, Madsen P, Pallesen LT, Christensen B, Sørensen ES, Nissen P, Petersen CM, Thirup SS (September 2014). "Revisiting the structure of the Vps10 domain of human sortilin and its interaction with neurotensin". Protein Science. 23 (9): 1291–300. doi:10.1002/pro.2512. PMC 4243999. PMID 24985322.
  17. ↑ Schmidt V, Willnow TE (February 2016). "Protein sorting gone wrong--VPS10P domain receptors in cardiovascular and metabolic diseases". Atherosclerosis. 245: 194–9. doi:10.1016/j.atherosclerosis.2015.11.027. PMID 26724530.
  18. ↑ Akil H, Perraud A, Mélin C, Jauberteau MO, Mathonnet M (2011-01-01). "Fine-tuning roles of endogenous brain-derived neurotrophic factor, TrkB and sortilin in colorectal cancer cell survival". PLoS One. 6 (9): e25097. doi:10.1371/journal.pone.0025097. PMC 3180371. PMID 21966426.
  19. ↑ Nielsen MS, Jacobsen C, Olivecrona G, Gliemann J, Petersen CM (March 1999). "Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase". The Journal of Biological Chemistry. 274 (13): 8832–6. doi:10.1074/jbc.274.13.8832. PMID 10085125.
  20. ↑ 20.0 20.1 Ariga M, Nedachi T, Katagiri H, Kanzaki M (April 2008). "Functional role of sortilin in myogenesis and development of insulin-responsive glucose transport system in C2C12 myocytes". The Journal of Biological Chemistry. 283 (15): 10208–20. doi:10.1074/jbc.M710604200. PMID 18258592.
  21. ↑ Maeda S, Nobukuni T, Shimo-Onoda K, Hayashi K, Yone K, Komiya S, Inoue I (October 2002). "Sortilin is upregulated during osteoblastic differentiation of mesenchymal stem cells and promotes extracellular matrix mineralization". Journal of Cellular Physiology. 193 (1): 73–9. doi:10.1002/jcp.10151. PMID 12209882.
  22. ↑ Strong A, Rader DJ (June 2012). "Sortilin as a regulator of lipoprotein metabolism". Current Atherosclerosis Reports. 14 (3): 211–8. doi:10.1007/s11883-012-0248-x. PMID 22538429.
  23. ↑ Zhong LY, Cayabyab FS, Tang CK, Zheng XL, Peng TH, Lv YC (September 2016). "Sortilin: A novel regulator in lipid metabolism and atherogenesis". Clinica Chimica Acta. 460: 11–7. doi:10.1016/j.cca.2016.06.013. PMID 27312323.
  24. ↑ Kjolby M, Andersen OM, Breiderhoff T, Fjorback AW, Pedersen KM, Madsen P, Jansen P, Heeren J, Willnow TE, Nykjaer A (September 2010). "Sort1, encoded by the cardiovascular risk locus 1p13.3, is a regulator of hepatic lipoprotein export". Cell Metabolism. 12 (3): 213–23. doi:10.1016/j.cmet.2010.08.006. PMID 20816088.
  25. ↑ 25.0 25.1 Carlo AS (2013-10-01). "Sortilin, a novel APOE receptor implicated in Alzheimer disease". Prion. 7 (5): 378–82. doi:10.4161/pri.26746. PMC 4134342. PMID 24121631.
  26. ↑ Jin C, Liu X, Zhang F, Wu Y, Yuan J, Zhu J, Zhang F, Wang G, Cheng Z (2013-01-01). "An updated meta-analysis of the association between SORL1 variants and the risk for sporadic Alzheimer's disease". Journal of Alzheimer's Disease. 37 (2): 429–37. doi:10.3233/JAD-130533. PMID 23948893.
  27. ↑ Piscopo P, Tosto G, Belli C, Talarico G, Galimberti D, Gasparini M, Canevelli M, Poleggi A, Crestini A, Albani D, Forloni G, Lucca U, Quadri P, Tettamanti M, Fenoglio C, Scarpini E, Bruno G, Vanacore N, Confaloni A (2015-01-01). "SORL1 Gene is Associated with the Conversion from Mild Cognitive Impairment to Alzheimer's Disease". Journal of Alzheimer's Disease. 46 (3): 771–6. doi:10.3233/JAD-141551. PMID 25881907.
  28. ↑ Andersson CH, Hansson O, Minthon L, Andreasen N, Blennow K, Zetterberg H, Skoog I, Wallin A, Nilsson S, Kettunen P (July 2016). "A Genetic Variant of the Sortilin 1 Gene is Associated with Reduced Risk of Alzheimer's Disease". Journal of Alzheimer's Disease. 53: 1353–63. doi:10.3233/JAD-160319. PMID 27392867.
  29. ↑ 29.0 29.1 Samani NJ, Erdmann J, Hall AS, Hengstenberg C, Mangino M, Mayer B, Dixon RJ, Meitinger T, Braund P, Wichmann HE, Barrett JH, König IR, Stevens SE, Szymczak S, Tregouet DA, Iles MM, Pahlke F, Pollard H, Lieb W, Cambien F, Fischer M, Ouwehand W, Blankenberg S, Balmforth AJ, Baessler A, Ball SG, Strom TM, Braenne I, Gieger C, Deloukas P, Tobin MD, Ziegler A, Thompson JR, Schunkert H (August 2007). "Genomewide association analysis of coronary artery disease". The New England Journal of Medicine. 357 (5): 443–53. doi:10.1056/NEJMoa072366. PMC 2719290. PMID 17634449.
  30. ↑ Nikpay M, Goel A, Won HH, Hall LM, Willenborg C, Kanoni S, et al. (October 2015). "A comprehensive 1,000 Genomes-based genome-wide association meta-analysis of coronary artery disease". Nature Genetics. 47 (10): 1121–30. doi:10.1038/ng.3396. PMC 4589895. PMID 26343387.
  31. ↑ Zeller T, Blankenberg S, Diemert P (January 2012). "Genomewide association studies in cardiovascular disease--an update 2011". Clinical Chemistry. 58 (1): 92–103. doi:10.1373/clinchem.2011.170431. PMID 22125304.
  32. ↑ 32.0 32.1 Ogawa K, Ueno T, Iwasaki T, Kujiraoka T, Ishihara M, Kunimoto S, Takayama T, Kanai T, Hirayama A, Hattori H (June 2016). "Soluble sortilin is released by activated platelets and its circulating levels are associated with cardiovascular risk factors". Atherosclerosis. 249: 110–5. doi:10.1016/j.atherosclerosis.2016.03.041. PMID 27085161.
  33. ↑ 33.0 33.1 Jacobsen L, Madsen P, Nielsen MS, Geraerts WP, Gliemann J, Smit AB, Petersen CM (January 2002). "The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding". FEBS Letters. 511 (1–3): 155–8. doi:10.1016/S0014-5793(01)03299-9. PMID 11821067.

Further reading

  • Vincent JP, Mazella J, Kitabgi P (July 1999). "Neurotensin and neurotensin receptors". Trends in Pharmacological Sciences. 20 (7): 302–9. doi:10.1016/S0165-6147(99)01357-7. PMID 10390649.
  • Mazella J (January 2001). "Sortilin/neurotensin receptor-3: a new tool to investigate neurotensin signaling and cellular trafficking?". Cellular Signalling. 13 (1): 1–6. doi:10.1016/S0898-6568(00)00130-3. PMID 11257441.
  • Petersen CM, Nielsen MS, Nykjaer A, Jacobsen L, Tommerup N, Rasmussen HH, Roigaard H, Gliemann J, Madsen P, Moestrup SK (February 1997). "Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography". The Journal of Biological Chemistry. 272 (6): 3599–605. doi:10.1074/jbc.272.6.3599. PMID 9013611.
  • Lin BZ, Pilch PF, Kandror KV (September 1997). "Sortilin is a major protein component of Glut4-containing vesicles". The Journal of Biological Chemistry. 272 (39): 24145–7. doi:10.1074/jbc.272.39.24145. PMID 9305862.
  • Tauris J, Ellgaard L, Jacobsen C, Nielsen MS, Madsen P, Thøgersen HC, Gliemann J, Petersen CM, Moestrup SK (June 1998). "The carboxy-terminal domain of the receptor-associated protein binds to the Vps10p domain of sortilin". FEBS Letters. 429 (1): 27–30. doi:10.1016/S0014-5793(98)00559-6. PMID 9657377.
  • Mazella J, Zsürger N, Navarro V, Chabry J, Kaghad M, Caput D, Ferrara P, Vita N, Gully D, Maffrand JP, Vincent JP (October 1998). "The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor". The Journal of Biological Chemistry. 273 (41): 26273–6. doi:10.1074/jbc.273.41.26273. PMID 9756851.
  • Munck Petersen C, Nielsen MS, Jacobsen C, Tauris J, Jacobsen L, Gliemann J, Moestrup SK, Madsen P (February 1999). "Propeptide cleavage conditions sortilin/neurotensin receptor-3 for ligand binding". The EMBO Journal. 18 (3): 595–604. doi:10.1093/emboj/18.3.595. PMC 1171152. PMID 9927419.
  • Nielsen MS, Jacobsen C, Olivecrona G, Gliemann J, Petersen CM (March 1999). "Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase". The Journal of Biological Chemistry. 274 (13): 8832–6. doi:10.1074/jbc.274.13.8832. PMID 10085125.
  • Nielsen MS, Madsen P, Christensen EI, Nykjaer A, Gliemann J, Kasper D, Pohlmann R, Petersen CM (May 2001). "The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein". The EMBO Journal. 20 (9): 2180–90. doi:10.1093/emboj/20.9.2180. PMC 125444. PMID 11331584.
  • Takatsu H, Katoh Y, Shiba Y, Nakayama K (July 2001). "Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains". The Journal of Biological Chemistry. 276 (30): 28541–5. doi:10.1074/jbc.C100218200. PMID 11390366.
  • Hampe W, Rezgaoui M, Hermans-Borgmeyer I, Schaller HC (June 2001). "The genes for the human VPS10 domain-containing receptors are large and contain many small exons". Human Genetics. 108 (6): 529–36. doi:10.1007/s004390100504. PMID 11499680.
  • Shiba T, Takatsu H, Nogi T, Matsugaki N, Kawasaki M, Igarashi N, Suzuki M, Kato R, Earnest T, Nakayama K, Wakatsuki S (February 2002). "Structural basis for recognition of acidic-cluster dileucine sequence by GGA1". Nature. 415 (6874): 937–41. doi:10.1038/415937a. PMID 11859376.
  • Maeda S, Nobukuni T, Shimo-Onoda K, Hayashi K, Yone K, Komiya S, Inoue I (October 2002). "Sortilin is upregulated during osteoblastic differentiation of mesenchymal stem cells and promotes extracellular matrix mineralization". Journal of Cellular Physiology. 193 (1): 73–9. doi:10.1002/jcp.10151. PMID 12209882.
  • Martin S, Navarro V, Vincent JP, Mazella J (October 2002). "Neurotensin receptor-1 and -3 complex modulates the cellular signaling of neurotensin in the HT29 cell line". Gastroenterology. 123 (4): 1135–43. doi:10.1053/gast.2002.36000. PMID 12360476.
  • Navarro V, Vincent JP, Mazella J (November 2002). "Shedding of the luminal domain of the neurotensin receptor-3/sortilin in the HT29 cell line". Biochemical and Biophysical Research Communications. 298 (5): 760–4. doi:10.1016/S0006-291X(02)02564-0. PMID 12419319.
  • Martin S, Vincent JP, Mazella J (February 2003). "Involvement of the neurotensin receptor-3 in the neurotensin-induced migration of human microglia". The Journal of Neuroscience. 23 (4): 1198–205. PMID 12598608.
  • Lefrancois S, Zeng J, Hassan AJ, Canuel M, Morales CR (December 2003). "The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin". The EMBO Journal. 22 (24): 6430–7. doi:10.1093/emboj/cdg629. PMC 291824. PMID 14657016.
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