PSMA7: Difference between revisions

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'''Proteasome subunit alpha type-7''' also known as '''20S proteasome subunit alpha-4'''  is a [[protein]] that in humans is encoded by the ''PSMA7'' [[gene]].<ref name="pmid8764072">{{cite journal | vauthors = Huang J, Kwong J, Sun EC, Liang TJ | title = Proteasome complex as a potential cellular target of hepatitis B virus X protein | journal = Journal of Virology | volume = 70 | issue = 8 | pages = 5582–91 | date = August 1996 | pmid = 8764072 | pmc = 190518 | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PSMA7 proteasome (prosome, macropain) subunit, alpha type, 7| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5688| accessdate = }}</ref> This protein is one of the 17 essential subunits (alpha subunits 1-7, constitutive beta subunits 1-7, and inducible subunits including beta1i, beta2i, beta5i) that contributes to the complete assembly of 20S proteasome complex.
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PSMA7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1iru.
| PDB = {{PDB2|1iru}}
| Name = Proteasome (prosome, macropain) subunit, alpha type, 7
| HGNCid = 9536
| Symbol = PSMA7
| AltSymbols =; C6; HSPC; MGC3755; RC6-1; XAPC7
| OMIM = 606607
| ECnumber = 
| Homologene = 2086
| MGIid = 1347070
| GeneAtlas_image1 = PBB_GE_PSMA7_216088_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSMA7_201114_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004298 |text = threonine endopeptidase activity}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005839 |text = proteasome core complex (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5688
    | Hs_Ensembl = ENSG00000101182
    | Hs_RefseqProtein = NP_002783
    | Hs_RefseqmRNA = NM_002792
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 60145186
    | Hs_GenLoc_end = 60151881
    | Hs_Uniprot = O14818
    | Mm_EntrezGene = 26444
    | Mm_Ensembl = ENSMUSG00000027566
    | Mm_RefseqmRNA = NM_011969
    | Mm_RefseqProtein = NP_036099
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 179965784
    | Mm_GenLoc_end = 179971816
    | Mm_Uniprot = Q3THL2
  }}
}}
'''Proteasome (prosome, macropain) subunit, alpha type, 7''', also known as '''PSMA7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMA7 proteasome (prosome, macropain) subunit, alpha type, 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5688| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The eukaryotic proteasome recognized degradable proteins, including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes. An essential function of a modified proteasome, the immunoproteasome, is the processing of [[class I MHC]] peptides. As a component of alpha ring, proteasome subunit alpha type-7 contributes to the formation of heptameric alpha rings and substrate entrance gate. Importantly, this subunit plays an critical role in the assembly of 19S base and 20S. This particular subunit has been shown to interact specifically with the hepatitis B virus X protein, a protein critical to viral replication. In addition, this subunit is involved in regulating hepatitis virus C internal ribosome entry site (IRES) activity, an activity essential for viral replication. This core alpha subunit is also involved in regulating the hypoxia-inducible factor-1alpha, a transcription factor important for cellular responses to oxygen tension. Recent study on underlying mechanisms of E3 ligase Parkin-related neurodegeneration identified this proteasome subunit as one of [[Parkin (ligase)|Parkin]] associating partner. The protein-protein interaction was initiated between the C-terminal domain of Parkin and C-terminal of subunit alpha4 (systematic nomenclature).<ref>{{cite journal | vauthors = Dächsel JC, Lücking CB, Deeg S, Schultz E, Lalowski M, Casademunt E, Corti O, Hampe C, Patenge N, Vaupel K, Yamamoto A, Dichgans M, Brice A, Wanker EE, Kahle PJ, Gasser T | title = Parkin interacts with the proteasome subunit alpha4 | journal = FEBS Letters | volume = 579 | issue = 18 | pages = 3913–9 | date = July 2005 | pmid = 15987638 | doi = 10.1016/j.febslet.2005.06.003 }}</ref>
{{PBB_Summary
| section_title =
| summary_text = The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. This particular subunit has been shown to interact specifically with the hepatitis B virus X protein, a protein critical to viral replication. In addition, this subunit is involved in regulating hepatitis virus C internal ribosome entry site (IRES) activity, an activity essential for viral replication. This core alpha subunit is also involved in regulating the hypoxia-inducible factor-1alpha, a transcription factor important for cellular responses to oxygen tension. Multiple isoforms of this subunit arising from alternative splicing may exist but alternative transcripts for only two isoforms have been defined. A pseudogene has been identified on chromosome 9.<ref name="entrez">{{cite web | title = Entrez Gene: PSMA7 proteasome (prosome, macropain) subunit, alpha type, 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5688| accessdate = }}</ref>
}}


==References==
== Structure ==
{{reflist|2}}
 
==Further reading==
=== Expression ===
{{refbegin | 2}}
 
{{PBB_Further_reading
The gene ''PSMA7'' encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. This gene has 7 exons and locates at a chromosome band 20q13.33. Multiple isoforms of this subunit arising from alternative splicing may exist but alternative transcripts for only two isoforms have been defined. A pseudogene has been identified on chromosome 9.<ref name="entrez"/>
| citations =
 
*{{cite journal  | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue=  |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
The human protein Proteasome subunit alpha type-7 is 28 kDa in size and composed of 248 amino acids. The calculated theoretical pI ([[Isoelectric point]]) of this protein is 8.60.
*{{cite journal  | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi=  }}
 
*{{cite journal | author=Kristensen P, Johnsen AH, Uerkvitz W, ''et al.'' |title=Human proteasome subunits from 2-dimensional gels identified by partial sequencing. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1785-9 |year= 1995 |pmid= 7811265 |doi= }}
=== Complex assembly ===
*{{cite journal | author=Akioka H, Forsberg NE, Ishida N, ''et al.'' |title=Isolation and characterization of the HC8 subunit gene of the human proteasome. |journal=Biochem. Biophys. Res. Commun. |volume=207 |issue= 1 |pages= 318-23 |year= 1995 |pmid= 7857283 |doi= 10.1006/bbrc.1995.1190 }}
 
*{{cite journal  | author=Huang J, Kwong J, Sun EC, Liang TJ |title=Proteasome complex as a potential cellular target of hepatitis B virus X protein. |journal=J. Virol. |volume=70 |issue= 8 |pages= 5582-91 |year= 1996 |pmid= 8764072 |doi= }}
The [[proteasome]] is a multicatalytic proteinase complex with a highly ordered 20S core structure. This barrel-shaped core structure is composed of 4 axially stacked rings of 28 non-identical subunits: the two end rings are each formed by 7 alpha subunits, and the two central rings are each formed by 7 beta subunits. Three beta subunits (beta1, beta2, and beta5) each contains a proteolytic active site and has distinct substrate preferences. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway.<ref>{{cite journal | vauthors = Coux O, Tanaka K, Goldberg AL | title = Structure and functions of the 20S and 26S proteasomes | journal = Annual Review of Biochemistry | volume = 65 | pages = 801–47 | date = 1996 | pmid = 8811196 | doi = 10.1146/annurev.bi.65.070196.004101 }}</ref><ref name="ReferenceB">{{cite journal | vauthors = Tomko RJ, Hochstrasser M | title = Molecular architecture and assembly of the eukaryotic proteasome | journal = Annual Review of Biochemistry | volume = 82 | pages = 415–45 | date = 2013 | pmid = 23495936 | pmc = 3827779 | doi = 10.1146/annurev-biochem-060410-150257 }}</ref>
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
 
*{{cite journal  | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
== Mechanism ==
*{{cite journal  | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
 
*{{cite journal | author=Elenich LA, Nandi D, Kent AE, ''et al.'' |title=The complete primary structure of mouse 20S proteasomes. |journal=Immunogenetics |volume=49 |issue= 10 |pages= 835-42 |year= 1999 |pmid= 10436176 |doi= }}
Crystal structures of isolated 20S proteasome complex demonstrate that the two rings of beta subunits form a proteolytic chamber and maintain all their active sites of proteolysis within the chamber.<ref name="ReferenceB"/> Concomitantly, the rings of alpha subunits form the entrance for substrates entering the proteolytic chamber. In an inactivated 20S proteasome complex, the gate into the internal proteolytic chamber are guarded by the N-terminal tails of specific alpha-subunit.<ref>{{cite journal | vauthors = Groll M, Ditzel L, Löwe J, Stock D, Bochtler M, Bartunik HD, Huber R | title = Structure of 20S proteasome from yeast at 2.4 A resolution | journal = Nature | volume = 386 | issue = 6624 | pages = 463–71 | date = April 1997 | pmid = 9087403 | doi = 10.1038/386463a0 | bibcode = 1997Natur.386..463G }}</ref><ref name="ReferenceA">{{cite journal | vauthors = Groll M, Bajorek M, Köhler A, Moroder L, Rubin DM, Huber R, Glickman MH, Finley D | title = A gated channel into the proteasome core particle | journal = Nature Structural Biology | volume = 7 | issue = 11 | pages = 1062–7 | date = November 2000 | pmid = 11062564 | doi = 10.1038/80992 }}</ref> The proteolytic capacity of 20S core particle (CP) can be activated when CP associates with one or two regulatory particles (RP) on one or both side of alpha rings. These regulatory particles include 19S proteasome complexes, 11S proteasome complex, etc. Following the CP-RP association, the confirmation of certain alpha subunits will change and consequently cause the opening of substrate entrance gate. Besides RPs, the 20S proteasomes can also be effectively activated by other mild chemical treatments, such as exposure to low levels of sodium dodecylsulfate (SDS) or NP-14.<ref name="ReferenceA"/><ref>{{cite journal | vauthors = Zong C, Gomes AV, Drews O, Li X, Young GW, Berhane B, Qiao X, French SW, Bardag-Gorce F, Ping P | title = Regulation of murine cardiac 20S proteasomes: role of associating partners | journal = Circulation Research | volume = 99 | issue = 4 | pages = 372–80 | date = August 2006 | pmid = 16857963 | doi = 10.1161/01.RES.0000237389.40000.02 }}</ref>
*{{cite journal  | author=Zhang Z, Torii N, Furusaka A, ''et al.'' |title=Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex. |journal=J. Biol. Chem. |volume=275 |issue= 20 |pages= 15157-65 |year= 2000 |pmid= 10748218 |doi= 10.1074/jbc.M910378199 }}
 
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
== Clinical significance ==
*{{cite journal | author=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi= }}
 
*{{cite journal | author=Feng Y, Longo DL, Ferris DK |title=Polo-like kinase interacts with proteasomes and regulates their activity. |journal=Cell Growth Differ. |volume=12 |issue= 1 |pages= 29-37 |year= 2001 |pmid= 11205743 |doi= }}
The Proteasome and its subunits are of clinical significance for at least two reasons: (1) a compromised complex assembly or a dysfunctional proteasome can be associated with the underlying pathophysiology of specific diseases, and (2) they can be exploited as drug targets for therapeutic interventions. More recently, more effort has been made to consider the proteasome for the development of novel diagnostic markers and strategies. An improved and comprehensive understanding of the pathophysiology of the proteasome should lead to clinical applications in the future.
*{{cite journal | author=Golubnitschaja-Labudova O, Liu R, Decker C, ''et al.'' |title=Altered gene expression in lymphocytes of patients with normal-tension glaucoma. |journal=Curr. Eye Res. |volume=21 |issue= 5 |pages= 867-76 |year= 2001 |pmid= 11262608 |doi= }}
 
*{{cite journal | author=Hartmann-Petersen R, Tanaka K, Hendil KB |title=Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking. |journal=Arch. Biochem. Biophys. |volume=386 |issue= 1 |pages= 89-94 |year= 2001 |pmid= 11361004 |doi= 10.1006/abbi.2000.2178 }}
The proteasomes form a pivotal component for the [[proteasome|Ubiquitin-Proteasome System (UPS)]] <ref>{{cite journal | vauthors = Kleiger G, Mayor T | title = Perilous journey: a tour of the ubiquitin-proteasome system | journal = Trends in Cell Biology | volume = 24 | issue = 6 | pages = 352–9 | date = June 2014 | pmid = 24457024 | pmc = 4037451 | doi = 10.1016/j.tcb.2013.12.003 }}</ref> and corresponding cellular Protein Quality Control (PQC). Protein [[ubiquitination]] and subsequent [[proteolysis]] and degradation by the proteasome are important mechanisms in the regulation of the [[cell cycle]], [[cell growth]] and differentiation, gene transcription, signal transduction and [[apoptosis]].<ref>{{cite journal | vauthors = Goldberg AL, Stein R, Adams J | title = New insights into proteasome function: from archaebacteria to drug development | journal = Chemistry & Biology | volume = 2 | issue = 8 | pages = 503–8 | date = August 1995 | pmid = 9383453 | doi = 10.1016/1074-5521(95)90182-5 }}</ref> Subsequently, a compromised proteasome complex assembly and function lead to reduced proteolytic activities and the accumulation of damaged or misfolded protein species. Such protein accumulation may contribute to the pathogenesis and phenotypic characteristics in neurodegenerative diseases,<ref>{{cite journal | vauthors = Sulistio YA, Heese K | title = The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease | journal = Molecular Neurobiology | volume = 53 | issue = 2 | pages = 905–31 | date = March 2016 | pmid = 25561438 | doi = 10.1007/s12035-014-9063-4 }}</ref><ref>{{cite journal | vauthors = Ortega Z, Lucas JJ | title = Ubiquitin-proteasome system involvement in Huntington's disease | journal = Frontiers in Molecular Neuroscience | volume = 7 | pages = 77 | date = 2014 | pmid = 25324717 | pmc = 4179678 | doi = 10.3389/fnmol.2014.00077 }}</ref> cardiovascular diseases,<ref>{{cite journal | vauthors = Sandri M, Robbins J | title = Proteotoxicity: an underappreciated pathology in cardiac disease | journal = Journal of Molecular and Cellular Cardiology | volume = 71 | pages = 3–10 | date = June 2014 | pmid = 24380730 | pmc = 4011959 | doi = 10.1016/j.yjmcc.2013.12.015 }}</ref><ref>{{cite journal | vauthors = Drews O, Taegtmeyer H | title = Targeting the ubiquitin-proteasome system in heart disease: the basis for new therapeutic strategies | journal = Antioxidants & Redox Signaling | volume = 21 | issue = 17 | pages = 2322–43 | date = December 2014 | pmid = 25133688 | pmc = 4241867 | doi = 10.1089/ars.2013.5823 }}</ref><ref>{{cite journal | vauthors = Wang ZV, Hill JA | title = Protein quality control and metabolism: bidirectional control in the heart | journal = Cell Metabolism | volume = 21 | issue = 2 | pages = 215–26 | date = February 2015 | pmid = 25651176 | pmc = 4317573 | doi = 10.1016/j.cmet.2015.01.016 }}</ref> inflammatory responses and autoimmune diseases,<ref name="Karin M 2000">{{cite journal | vauthors = Karin M, Delhase M | title = The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signalling | journal = Seminars in Immunology | volume = 12 | issue = 1 | pages = 85–98 | date = February 2000 | pmid = 10723801 | doi = 10.1006/smim.2000.0210 }}</ref>  and systemic DNA damage responses leading to [[malignancies]].<ref>{{cite journal | vauthors = Ermolaeva MA, Dakhovnik A, Schumacher B | title = Quality control mechanisms in cellular and systemic DNA damage responses | journal = Ageing Research Reviews | volume = 23 | issue = Pt A | pages = 3–11 | date = September 2015 | pmid = 25560147 | doi = 10.1016/j.arr.2014.12.009 | pmc=4886828}}</ref>
*{{cite journal | author=Cho S, Choi YJ, Kim JM, ''et al.'' |title=Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7. |journal=FEBS Lett. |volume=498 |issue= 1 |pages= 62-6 |year= 2001 |pmid= 11389899 |doi= }}
 
*{{cite journal | author=Krüger M, Beger C, Welch PJ, ''et al.'' |title=Involvement of proteasome alpha-subunit PSMA7 in hepatitis C virus internal ribosome entry site-mediated translation. |journal=Mol. Cell. Biol. |volume=21 |issue= 24 |pages= 8357-64 |year= 2001 |pmid= 11713272 |doi= 10.1128/MCB.21.24.8357-8364.2001 }}
Several experimental and clinical studies have indicated that aberrations and deregulations of the UPS contribute to the pathogenesis of several neurodegenerative and myodegenerative disorders, including [[Alzheimer's disease]],<ref>{{cite journal | vauthors = Checler F, da Costa CA, Ancolio K, Chevallier N, Lopez-Perez E, Marambaud P | title = Role of the proteasome in Alzheimer's disease | journal = Biochimica et Biophysica Acta | volume = 1502 | issue = 1 | pages = 133–8 | date = July 2000 | pmid = 10899438 | doi = 10.1016/s0925-4439(00)00039-9 }}</ref> [[Parkinson's disease]]<ref name="ReferenceC">{{cite journal | vauthors = Chung KK, Dawson VL, Dawson TM | title = The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders | journal = Trends in Neurosciences | volume = 24 | issue = 11 Suppl | pages = S7-14 | date = November 2001 | pmid = 11881748 | doi = 10.1016/s0166-2236(00)01998-6 }}</ref> and [[Pick's disease]],<ref name="IkedaAkiyama2002">{{cite journal | vauthors = Ikeda K, Akiyama H, Arai T, Ueno H, Tsuchiya K, Kosaka K | title = Morphometrical reappraisal of motor neuron system of Pick's disease and amyotrophic lateral sclerosis with dementia | journal = Acta Neuropathologica | volume = 104 | issue = 1 | pages = 21–8 | date = July 2002 | pmid = 12070660 | doi = 10.1007/s00401-001-0513-5 }}</ref> [[Amyotrophic lateral sclerosis]] ([[ALS]]),<ref name="IkedaAkiyama2002"/> [[Huntington's disease]],<ref name="ReferenceC"/> [[Creutzfeldt–Jakob disease]],<ref>{{cite journal | vauthors = Manaka H, Kato T, Kurita K, Katagiri T, Shikama Y, Kujirai K, Kawanami T, Suzuki Y, Nihei K, Sasaki H | title = Marked increase in cerebrospinal fluid ubiquitin in Creutzfeldt-Jakob disease | journal = Neuroscience Letters | volume = 139 | issue = 1 | pages = 47–9 | date = May 1992 | pmid = 1328965 | doi = 10.1016/0304-3940(92)90854-z }}</ref> and motor neuron diseases, polyglutamine (PolyQ) diseases, [[Muscular dystrophies]]<ref>{{cite journal | vauthors = Mathews KD, Moore SA | title = Limb-girdle muscular dystrophy | journal = Current Neurology and Neuroscience Reports | volume = 3 | issue = 1 | pages = 78–85 | date = January 2003 | pmid = 12507416 | doi = 10.1007/s11910-003-0042-9 }}</ref> and several rare forms of neurodegenerative diseases associated with [[dementia]].<ref>{{cite journal | vauthors = Mayer RJ | title = From neurodegeneration to neurohomeostasis: the role of ubiquitin | journal = Drug News & Perspectives | volume = 16 | issue = 2 | pages = 103–8 | date = March 2003 | pmid = 12792671 | doi = 10.1358/dnp.2003.16.2.829327 }}</ref> As part of the [[proteasome|Ubiquitin-Proteasome System (UPS)]], the proteasome maintains cardiac protein homeostasis and thus plays a significant role in cardiac [[Ischemic]] injury,<ref>{{cite journal | vauthors = Calise J, Powell SR | title = The ubiquitin proteasome system and myocardial ischemia | journal = American Journal of Physiology. Heart and Circulatory Physiology | volume = 304 | issue = 3 | pages = H337-49 | date = February 2013 | pmid = 23220331 | pmc = 3774499 | doi = 10.1152/ajpheart.00604.2012 }}</ref> [[ventricular hypertrophy]]<ref>{{cite journal | vauthors = Predmore JM, Wang P, Davis F, Bartolone S, Westfall MV, Dyke DB, Pagani F, Powell SR, Day SM | title = Ubiquitin proteasome dysfunction in human hypertrophic and dilated cardiomyopathies | journal = Circulation | volume = 121 | issue = 8 | pages = 997–1004 | date = March 2010 | pmid = 20159828 | pmc = 2857348 | doi = 10.1161/CIRCULATIONAHA.109.904557 }}</ref> and [[Heart failure]].<ref>{{cite journal | vauthors = Powell SR | title = The ubiquitin-proteasome system in cardiac physiology and pathology | journal = American Journal of Physiology. Heart and Circulatory Physiology | volume = 291 | issue = 1 | pages = H1-H19 | date = July 2006 | pmid = 16501026 | doi = 10.1152/ajpheart.00062.2006 }}</ref> Additionally, evidence is accumulating that the UPS plays an essential role in malignant transformation. UPS proteolysis plays a major role in responses of cancer cells to stimulatory signals that are critical for the development of cancer. Accordingly, gene expression by degradation of [[transcription factors]], such as [[p53]], [[c-Jun]], [[c-Fos]], [[NF-κB]], [[c-Myc]], HIF-1α, MATα2, [[STAT3]], sterol-regulated element-binding proteins and [[androgen receptors]] are all controlled by the UPS and thus involved in the development of various malignancies.<ref>{{cite journal | vauthors = Adams J | title = Potential for proteasome inhibition in the treatment of cancer | journal = Drug Discovery Today | volume = 8 | issue = 7 | pages = 307–15 | date = April 2003 | pmid = 12654543 | doi = 10.1016/s1359-6446(03)02647-3 }}</ref> Moreover, the UPS regulates the degradation of tumor suppressor gene products such as [[adenomatous polyposis coli]] ([[adenomatous polyposis coli|APC]]) in colorectal cancer, [[retinoblastoma]] (Rb). and [[von Hippel-Lindau tumor suppressor]] (VHL), as well as a number of [[proto-oncogenes]] ([[Raf kinase|Raf]], [[Myc]], [[MYB (gene)|Myb]], [[NF-κB|Rel]], [[Src (gene)|Src]], [[MOS (gene)|Mos]], [[Abl (gene)|Abl]]). The UPS is also involved in the regulation of inflammatory responses. This activity is usually attributed to the role of proteasomes in the activation of NF-κB which further regulates the expression of pro inflammatory [[cytokines]] such as [[TNF-α]], IL-β, [[Interleukin 8|IL-8]], [[adhesion molecules]] ([[ICAM-1]], [[VCAM-1]], P selectine) and [[prostaglandins]] and [[nitric oxide]] (NO).<ref name="Karin M 2000"/> Additionally, the UPS also plays a role in inflammatory responses as regulators of leukocyte proliferation, mainly through proteolysis of cyclines and the degradation of [[Cyclin-dependent kinase|CDK]] inhibitors.<ref>{{cite journal | vauthors = Ben-Neriah Y | title = Regulatory functions of ubiquitination in the immune system | journal = Nature Immunology | volume = 3 | issue = 1 | pages = 20–6 | date = January 2002 | pmid = 11753406 | doi = 10.1038/ni0102-20 }}</ref> Lastly, [[autoimmune disease]] patients with [[Systemic lupus erythematosus|SLE]], [[Sjogren's syndrome]] and [[rheumatoid arthritis]] (RA) predominantly exhibit circulating proteasomes which can be applied as clinical biomarkers.<ref>{{cite journal | vauthors = Egerer K, Kuckelkorn U, Rudolph PE, Rückert JC, Dörner T, Burmester GR, Kloetzel PM, Feist E | title = Circulating proteasomes are markers of cell damage and immunologic activity in autoimmune diseases | journal = The Journal of Rheumatology | volume = 29 | issue = 10 | pages = 2045–52 | date = October 2002 | pmid = 12375310 }}</ref>
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
 
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
Reports have shown that the proteasome subunit alpha type-7 (PSMA7) is overexpressed in [[colorectal cancer]] and associated with its hepatic [[metastasis]].<ref>{{cite journal | vauthors = Hu XT, Chen W, Wang D, Shi QL, Zhang FB, Liao YQ, Jin M, He C | title = The proteasome subunit PSMA7 located on the 20q13 amplicon is overexpressed and associated with liver metastasis in colorectal cancer | journal = Oncology Reports | volume = 19 | issue = 2 | pages = 441–6 | date = February 2008 | pmid = 18202793 }}</ref><ref>{{cite journal | vauthors = Hu XT, Chen W, Zhang FB, Shi QL, Hu JB, Geng SM, He C | title = Depletion of the proteasome subunit PSMA7 inhibits colorectal cancer cell tumorigenicity and migration | journal = Oncology Reports | volume = 22 | issue = 5 | pages = 1247–52 | date = November 2009 | pmid = 19787246 }}</ref> It was further reported that PSMA7 is associated with nucleotide-binding oligomerization domain-containing protein 1 ([[NOD1]]) as a negative regulator and may promote tumor growth by its inhibitory role on NOD1.<ref>{{cite journal | vauthors = Yang L, Tang Z, Zhang H, Kou W, Lu Z, Li X, Li Q, Miao Z | title = PSMA7 directly interacts with NOD1 and regulates its function | journal = Cellular Physiology and Biochemistry | volume = 31 | issue = 6 | pages = 952–9 | date = 2013 | pmid = 23839082 | doi = 10.1159/000350113 }}</ref>
}}
 
== Interactions ==
 
PSMA7 has been shown to [[Protein-protein interaction|interact]] with [[HIF1A]]<ref name=pmid11389899>{{cite journal | vauthors = Cho S, Choi YJ, Kim JM, Jeong ST, Kim JH, Kim SH, Ryu SE | title = Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7 | journal = FEBS Letters | volume = 498 | issue = 1 | pages = 62–6 | date = June 2001 | pmid = 11389899 | doi = 10.1016/S0014-5793(01)02499-1 }}</ref> and [[PLK1]].<ref name=pmid11205743>{{cite journal | vauthors = Feng Y, Longo DL, Ferris DK | title = Polo-like kinase interacts with proteasomes and regulates their activity | journal = Cell Growth & Differentiation | volume = 12 | issue = 1 | pages = 29–37 | date = January 2001 | pmid = 11205743 }}</ref>
 
== References ==
{{reflist|33em}}
 
== Further reading ==
{{refbegin|33em}}
* {{cite journal | vauthors = Coux O, Tanaka K, Goldberg AL | title = Structure and functions of the 20S and 26S proteasomes | journal = Annual Review of Biochemistry | volume = 65 | issue =  | pages = 801–47 | year = 1996 | pmid = 8811196 | doi = 10.1146/annurev.bi.65.070196.004101 }}
* {{cite journal | vauthors = Goff SP | title = Death by deamination: a novel host restriction system for HIV-1 | journal = Cell | volume = 114 | issue = 3 | pages = 281–3 | date = August 2003 | pmid = 12914693 | doi = 10.1016/S0092-8674(03)00602-0 }}
* {{cite journal | vauthors = Kristensen P, Johnsen AH, Uerkvitz W, Tanaka K, Hendil KB | title = Human proteasome subunits from 2-dimensional gels identified by partial sequencing | journal = Biochemical and Biophysical Research Communications | volume = 205 | issue = 3 | pages = 1785–9 | date = December 1994 | pmid = 7811265 | doi = 10.1006/bbrc.1994.2876 }}
* {{cite journal | vauthors = Akioka H, Forsberg NE, Ishida N, Okumura K, Nogami M, Taguchi H, Noda C, Tanaka K | title = Isolation and characterization of the HC8 subunit gene of the human proteasome | journal = Biochemical and Biophysical Research Communications | volume = 207 | issue = 1 | pages = 318–23 | date = February 1995 | pmid = 7857283 | doi = 10.1006/bbrc.1995.1190 }}
* {{cite journal | vauthors = Seeger M, Ferrell K, Frank R, Dubiel W | title = HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation | journal = The Journal of Biological Chemistry | volume = 272 | issue = 13 | pages = 8145–8 | date = March 1997 | pmid = 9079628 | doi = 10.1074/jbc.272.13.8145 }}
* {{cite journal | vauthors = Madani N, Kabat D | title = An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein | journal = Journal of Virology | volume = 72 | issue = 12 | pages = 10251–5 | date = December 1998 | pmid = 9811770 | pmc = 110608 | doi =  }}
* {{cite journal | vauthors = Simon JH, Gaddis NC, Fouchier RA, Malim MH | title = Evidence for a newly discovered cellular anti-HIV-1 phenotype | journal = Nature Medicine | volume = 4 | issue = 12 | pages = 1397–400 | date = December 1998 | pmid = 9846577 | doi = 10.1038/3987 }}
* {{cite journal | vauthors = Elenich LA, Nandi D, Kent AE, McCluskey TS, Cruz M, Iyer MN, Woodward EC, Conn CW, Ochoa AL, Ginsburg DB, Monaco JJ | title = The complete primary structure of mouse 20S proteasomes | journal = Immunogenetics | volume = 49 | issue = 10 | pages = 835–42 | date = September 1999 | pmid = 10436176 | doi = 10.1007/s002510050562 }}
* {{cite journal | vauthors = Zhang Z, Torii N, Furusaka A, Malayaman N, Hu Z, Liang TJ | title = Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex | journal = The Journal of Biological Chemistry | volume = 275 | issue = 20 | pages = 15157–65 | date = May 2000 | pmid = 10748218 | doi = 10.1074/jbc.M910378199 }}
* {{cite journal | vauthors = Mulder LC, Muesing MA | title = Degradation of HIV-1 integrase by the N-end rule pathway | journal = The Journal of Biological Chemistry | volume = 275 | issue = 38 | pages = 29749–53 | date = September 2000 | pmid = 10893419 | doi = 10.1074/jbc.M004670200 }}
* {{cite journal | vauthors = Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z | title = Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells | journal = Genome Research | volume = 10 | issue = 10 | pages = 1546–60 | date = October 2000 | pmid = 11042152 | pmc = 310934 | doi = 10.1101/gr.140200 }}
* {{cite journal | vauthors = Feng Y, Longo DL, Ferris DK | title = Polo-like kinase interacts with proteasomes and regulates their activity | journal = Cell Growth & Differentiation | volume = 12 | issue = 1 | pages = 29–37 | date = January 2001 | pmid = 11205743 | doi =  }}
* {{cite journal | vauthors = Golubnitschaja-Labudova O, Liu R, Decker C, Zhu P, Haefliger IO, Flammer J | title = Altered gene expression in lymphocytes of patients with normal-tension glaucoma | journal = Current Eye Research | volume = 21 | issue = 5 | pages = 867–76 | date = November 2000 | pmid = 11262608 | doi = 10.1076/ceyr.21.5.867.5534 }}
* {{cite journal | vauthors = Hartmann-Petersen R, Tanaka K, Hendil KB | title = Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking | journal = Archives of Biochemistry and Biophysics | volume = 386 | issue = 1 | pages = 89–94 | date = February 2001 | pmid = 11361004 | doi = 10.1006/abbi.2000.2178 }}
* {{cite journal | vauthors = Cho S, Choi YJ, Kim JM, Jeong ST, Kim JH, Kim SH, Ryu SE | title = Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7 | journal = FEBS Letters | volume = 498 | issue = 1 | pages = 62–6 | date = June 2001 | pmid = 11389899 | doi = 10.1016/S0014-5793(01)02499-1 }}
* {{cite journal | vauthors = Krüger M, Beger C, Welch PJ, Barber JR, Manns MP, Wong-Staal F | title = Involvement of proteasome alpha-subunit PSMA7 in hepatitis C virus internal ribosome entry site-mediated translation | journal = Molecular and Cellular Biology | volume = 21 | issue = 24 | pages = 8357–64 | date = December 2001 | pmid = 11713272 | pmc = 100000 | doi = 10.1128/MCB.21.24.8357-8364.2001 }}
* {{cite journal | vauthors = Sheehy AM, Gaddis NC, Choi JD, Malim MH | title = Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein | journal = Nature | volume = 418 | issue = 6898 | pages = 646–50 | date = August 2002 | pmid = 12167863 | doi = 10.1038/nature00939 | bibcode = 2002Natur.418..646S }}
{{refend}}
{{refend}}


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{{Proteasome subunits}}

Revision as of 18:50, 7 September 2017

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Proteasome subunit alpha type-7 also known as 20S proteasome subunit alpha-4 is a protein that in humans is encoded by the PSMA7 gene.[1][2] This protein is one of the 17 essential subunits (alpha subunits 1-7, constitutive beta subunits 1-7, and inducible subunits including beta1i, beta2i, beta5i) that contributes to the complete assembly of 20S proteasome complex.

Function

The eukaryotic proteasome recognized degradable proteins, including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. As a component of alpha ring, proteasome subunit alpha type-7 contributes to the formation of heptameric alpha rings and substrate entrance gate. Importantly, this subunit plays an critical role in the assembly of 19S base and 20S. This particular subunit has been shown to interact specifically with the hepatitis B virus X protein, a protein critical to viral replication. In addition, this subunit is involved in regulating hepatitis virus C internal ribosome entry site (IRES) activity, an activity essential for viral replication. This core alpha subunit is also involved in regulating the hypoxia-inducible factor-1alpha, a transcription factor important for cellular responses to oxygen tension. Recent study on underlying mechanisms of E3 ligase Parkin-related neurodegeneration identified this proteasome subunit as one of Parkin associating partner. The protein-protein interaction was initiated between the C-terminal domain of Parkin and C-terminal of subunit alpha4 (systematic nomenclature).[3]

Structure

Expression

The gene PSMA7 encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. This gene has 7 exons and locates at a chromosome band 20q13.33. Multiple isoforms of this subunit arising from alternative splicing may exist but alternative transcripts for only two isoforms have been defined. A pseudogene has been identified on chromosome 9.[2]

The human protein Proteasome subunit alpha type-7 is 28 kDa in size and composed of 248 amino acids. The calculated theoretical pI (Isoelectric point) of this protein is 8.60.

Complex assembly

The proteasome is a multicatalytic proteinase complex with a highly ordered 20S core structure. This barrel-shaped core structure is composed of 4 axially stacked rings of 28 non-identical subunits: the two end rings are each formed by 7 alpha subunits, and the two central rings are each formed by 7 beta subunits. Three beta subunits (beta1, beta2, and beta5) each contains a proteolytic active site and has distinct substrate preferences. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway.[4][5]

Mechanism

Crystal structures of isolated 20S proteasome complex demonstrate that the two rings of beta subunits form a proteolytic chamber and maintain all their active sites of proteolysis within the chamber.[5] Concomitantly, the rings of alpha subunits form the entrance for substrates entering the proteolytic chamber. In an inactivated 20S proteasome complex, the gate into the internal proteolytic chamber are guarded by the N-terminal tails of specific alpha-subunit.[6][7] The proteolytic capacity of 20S core particle (CP) can be activated when CP associates with one or two regulatory particles (RP) on one or both side of alpha rings. These regulatory particles include 19S proteasome complexes, 11S proteasome complex, etc. Following the CP-RP association, the confirmation of certain alpha subunits will change and consequently cause the opening of substrate entrance gate. Besides RPs, the 20S proteasomes can also be effectively activated by other mild chemical treatments, such as exposure to low levels of sodium dodecylsulfate (SDS) or NP-14.[7][8]

Clinical significance

The Proteasome and its subunits are of clinical significance for at least two reasons: (1) a compromised complex assembly or a dysfunctional proteasome can be associated with the underlying pathophysiology of specific diseases, and (2) they can be exploited as drug targets for therapeutic interventions. More recently, more effort has been made to consider the proteasome for the development of novel diagnostic markers and strategies. An improved and comprehensive understanding of the pathophysiology of the proteasome should lead to clinical applications in the future.

The proteasomes form a pivotal component for the Ubiquitin-Proteasome System (UPS) [9] and corresponding cellular Protein Quality Control (PQC). Protein ubiquitination and subsequent proteolysis and degradation by the proteasome are important mechanisms in the regulation of the cell cycle, cell growth and differentiation, gene transcription, signal transduction and apoptosis.[10] Subsequently, a compromised proteasome complex assembly and function lead to reduced proteolytic activities and the accumulation of damaged or misfolded protein species. Such protein accumulation may contribute to the pathogenesis and phenotypic characteristics in neurodegenerative diseases,[11][12] cardiovascular diseases,[13][14][15] inflammatory responses and autoimmune diseases,[16] and systemic DNA damage responses leading to malignancies.[17]

Several experimental and clinical studies have indicated that aberrations and deregulations of the UPS contribute to the pathogenesis of several neurodegenerative and myodegenerative disorders, including Alzheimer's disease,[18] Parkinson's disease[19] and Pick's disease,[20] Amyotrophic lateral sclerosis (ALS),[20] Huntington's disease,[19] Creutzfeldt–Jakob disease,[21] and motor neuron diseases, polyglutamine (PolyQ) diseases, Muscular dystrophies[22] and several rare forms of neurodegenerative diseases associated with dementia.[23] As part of the Ubiquitin-Proteasome System (UPS), the proteasome maintains cardiac protein homeostasis and thus plays a significant role in cardiac Ischemic injury,[24] ventricular hypertrophy[25] and Heart failure.[26] Additionally, evidence is accumulating that the UPS plays an essential role in malignant transformation. UPS proteolysis plays a major role in responses of cancer cells to stimulatory signals that are critical for the development of cancer. Accordingly, gene expression by degradation of transcription factors, such as p53, c-Jun, c-Fos, NF-κB, c-Myc, HIF-1α, MATα2, STAT3, sterol-regulated element-binding proteins and androgen receptors are all controlled by the UPS and thus involved in the development of various malignancies.[27] Moreover, the UPS regulates the degradation of tumor suppressor gene products such as adenomatous polyposis coli (APC) in colorectal cancer, retinoblastoma (Rb). and von Hippel-Lindau tumor suppressor (VHL), as well as a number of proto-oncogenes (Raf, Myc, Myb, Rel, Src, Mos, Abl). The UPS is also involved in the regulation of inflammatory responses. This activity is usually attributed to the role of proteasomes in the activation of NF-κB which further regulates the expression of pro inflammatory cytokines such as TNF-α, IL-β, IL-8, adhesion molecules (ICAM-1, VCAM-1, P selectine) and prostaglandins and nitric oxide (NO).[16] Additionally, the UPS also plays a role in inflammatory responses as regulators of leukocyte proliferation, mainly through proteolysis of cyclines and the degradation of CDK inhibitors.[28] Lastly, autoimmune disease patients with SLE, Sjogren's syndrome and rheumatoid arthritis (RA) predominantly exhibit circulating proteasomes which can be applied as clinical biomarkers.[29]

Reports have shown that the proteasome subunit alpha type-7 (PSMA7) is overexpressed in colorectal cancer and associated with its hepatic metastasis.[30][31] It was further reported that PSMA7 is associated with nucleotide-binding oligomerization domain-containing protein 1 (NOD1) as a negative regulator and may promote tumor growth by its inhibitory role on NOD1.[32]

Interactions

PSMA7 has been shown to interact with HIF1A[33] and PLK1.[34]

References

  1. ↑ Huang J, Kwong J, Sun EC, Liang TJ (August 1996). "Proteasome complex as a potential cellular target of hepatitis B virus X protein". Journal of Virology. 70 (8): 5582–91. PMC 190518. PMID 8764072.
  2. ↑ 2.0 2.1 "Entrez Gene: PSMA7 proteasome (prosome, macropain) subunit, alpha type, 7".
  3. ↑ Dächsel JC, Lücking CB, Deeg S, Schultz E, Lalowski M, Casademunt E, Corti O, Hampe C, Patenge N, Vaupel K, Yamamoto A, Dichgans M, Brice A, Wanker EE, Kahle PJ, Gasser T (July 2005). "Parkin interacts with the proteasome subunit alpha4". FEBS Letters. 579 (18): 3913–9. doi:10.1016/j.febslet.2005.06.003. PMID 15987638.
  4. ↑ Coux O, Tanaka K, Goldberg AL (1996). "Structure and functions of the 20S and 26S proteasomes". Annual Review of Biochemistry. 65: 801–47. doi:10.1146/annurev.bi.65.070196.004101. PMID 8811196.
  5. ↑ 5.0 5.1 Tomko RJ, Hochstrasser M (2013). "Molecular architecture and assembly of the eukaryotic proteasome". Annual Review of Biochemistry. 82: 415–45. doi:10.1146/annurev-biochem-060410-150257. PMC 3827779. PMID 23495936.
  6. ↑ Groll M, Ditzel L, Löwe J, Stock D, Bochtler M, Bartunik HD, Huber R (April 1997). "Structure of 20S proteasome from yeast at 2.4 A resolution". Nature. 386 (6624): 463–71. Bibcode:1997Natur.386..463G. doi:10.1038/386463a0. PMID 9087403.
  7. ↑ 7.0 7.1 Groll M, Bajorek M, Köhler A, Moroder L, Rubin DM, Huber R, Glickman MH, Finley D (November 2000). "A gated channel into the proteasome core particle". Nature Structural Biology. 7 (11): 1062–7. doi:10.1038/80992. PMID 11062564.
  8. ↑ Zong C, Gomes AV, Drews O, Li X, Young GW, Berhane B, Qiao X, French SW, Bardag-Gorce F, Ping P (August 2006). "Regulation of murine cardiac 20S proteasomes: role of associating partners". Circulation Research. 99 (4): 372–80. doi:10.1161/01.RES.0000237389.40000.02. PMID 16857963.
  9. ↑ Kleiger G, Mayor T (June 2014). "Perilous journey: a tour of the ubiquitin-proteasome system". Trends in Cell Biology. 24 (6): 352–9. doi:10.1016/j.tcb.2013.12.003. PMC 4037451. PMID 24457024.
  10. ↑ Goldberg AL, Stein R, Adams J (August 1995). "New insights into proteasome function: from archaebacteria to drug development". Chemistry & Biology. 2 (8): 503–8. doi:10.1016/1074-5521(95)90182-5. PMID 9383453.
  11. ↑ Sulistio YA, Heese K (March 2016). "The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease". Molecular Neurobiology. 53 (2): 905–31. doi:10.1007/s12035-014-9063-4. PMID 25561438.
  12. ↑ Ortega Z, Lucas JJ (2014). "Ubiquitin-proteasome system involvement in Huntington's disease". Frontiers in Molecular Neuroscience. 7: 77. doi:10.3389/fnmol.2014.00077. PMC 4179678. PMID 25324717.
  13. ↑ Sandri M, Robbins J (June 2014). "Proteotoxicity: an underappreciated pathology in cardiac disease". Journal of Molecular and Cellular Cardiology. 71: 3–10. doi:10.1016/j.yjmcc.2013.12.015. PMC 4011959. PMID 24380730.
  14. ↑ Drews O, Taegtmeyer H (December 2014). "Targeting the ubiquitin-proteasome system in heart disease: the basis for new therapeutic strategies". Antioxidants & Redox Signaling. 21 (17): 2322–43. doi:10.1089/ars.2013.5823. PMC 4241867. PMID 25133688.
  15. ↑ Wang ZV, Hill JA (February 2015). "Protein quality control and metabolism: bidirectional control in the heart". Cell Metabolism. 21 (2): 215–26. doi:10.1016/j.cmet.2015.01.016. PMC 4317573. PMID 25651176.
  16. ↑ 16.0 16.1 Karin M, Delhase M (February 2000). "The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signalling". Seminars in Immunology. 12 (1): 85–98. doi:10.1006/smim.2000.0210. PMID 10723801.
  17. ↑ Ermolaeva MA, Dakhovnik A, Schumacher B (September 2015). "Quality control mechanisms in cellular and systemic DNA damage responses". Ageing Research Reviews. 23 (Pt A): 3–11. doi:10.1016/j.arr.2014.12.009. PMC 4886828. PMID 25560147.
  18. ↑ Checler F, da Costa CA, Ancolio K, Chevallier N, Lopez-Perez E, Marambaud P (July 2000). "Role of the proteasome in Alzheimer's disease". Biochimica et Biophysica Acta. 1502 (1): 133–8. doi:10.1016/s0925-4439(00)00039-9. PMID 10899438.
  19. ↑ 19.0 19.1 Chung KK, Dawson VL, Dawson TM (November 2001). "The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders". Trends in Neurosciences. 24 (11 Suppl): S7–14. doi:10.1016/s0166-2236(00)01998-6. PMID 11881748.
  20. ↑ 20.0 20.1 Ikeda K, Akiyama H, Arai T, Ueno H, Tsuchiya K, Kosaka K (July 2002). "Morphometrical reappraisal of motor neuron system of Pick's disease and amyotrophic lateral sclerosis with dementia". Acta Neuropathologica. 104 (1): 21–8. doi:10.1007/s00401-001-0513-5. PMID 12070660.
  21. ↑ Manaka H, Kato T, Kurita K, Katagiri T, Shikama Y, Kujirai K, Kawanami T, Suzuki Y, Nihei K, Sasaki H (May 1992). "Marked increase in cerebrospinal fluid ubiquitin in Creutzfeldt-Jakob disease". Neuroscience Letters. 139 (1): 47–9. doi:10.1016/0304-3940(92)90854-z. PMID 1328965.
  22. ↑ Mathews KD, Moore SA (January 2003). "Limb-girdle muscular dystrophy". Current Neurology and Neuroscience Reports. 3 (1): 78–85. doi:10.1007/s11910-003-0042-9. PMID 12507416.
  23. ↑ Mayer RJ (March 2003). "From neurodegeneration to neurohomeostasis: the role of ubiquitin". Drug News & Perspectives. 16 (2): 103–8. doi:10.1358/dnp.2003.16.2.829327. PMID 12792671.
  24. ↑ Calise J, Powell SR (February 2013). "The ubiquitin proteasome system and myocardial ischemia". American Journal of Physiology. Heart and Circulatory Physiology. 304 (3): H337–49. doi:10.1152/ajpheart.00604.2012. PMC 3774499. PMID 23220331.
  25. ↑ Predmore JM, Wang P, Davis F, Bartolone S, Westfall MV, Dyke DB, Pagani F, Powell SR, Day SM (March 2010). "Ubiquitin proteasome dysfunction in human hypertrophic and dilated cardiomyopathies". Circulation. 121 (8): 997–1004. doi:10.1161/CIRCULATIONAHA.109.904557. PMC 2857348. PMID 20159828.
  26. ↑ Powell SR (July 2006). "The ubiquitin-proteasome system in cardiac physiology and pathology". American Journal of Physiology. Heart and Circulatory Physiology. 291 (1): H1–H19. doi:10.1152/ajpheart.00062.2006. PMID 16501026.
  27. ↑ Adams J (April 2003). "Potential for proteasome inhibition in the treatment of cancer". Drug Discovery Today. 8 (7): 307–15. doi:10.1016/s1359-6446(03)02647-3. PMID 12654543.
  28. ↑ Ben-Neriah Y (January 2002). "Regulatory functions of ubiquitination in the immune system". Nature Immunology. 3 (1): 20–6. doi:10.1038/ni0102-20. PMID 11753406.
  29. ↑ Egerer K, Kuckelkorn U, Rudolph PE, Rückert JC, Dörner T, Burmester GR, Kloetzel PM, Feist E (October 2002). "Circulating proteasomes are markers of cell damage and immunologic activity in autoimmune diseases". The Journal of Rheumatology. 29 (10): 2045–52. PMID 12375310.
  30. ↑ Hu XT, Chen W, Wang D, Shi QL, Zhang FB, Liao YQ, Jin M, He C (February 2008). "The proteasome subunit PSMA7 located on the 20q13 amplicon is overexpressed and associated with liver metastasis in colorectal cancer". Oncology Reports. 19 (2): 441–6. PMID 18202793.
  31. ↑ Hu XT, Chen W, Zhang FB, Shi QL, Hu JB, Geng SM, He C (November 2009). "Depletion of the proteasome subunit PSMA7 inhibits colorectal cancer cell tumorigenicity and migration". Oncology Reports. 22 (5): 1247–52. PMID 19787246.
  32. ↑ Yang L, Tang Z, Zhang H, Kou W, Lu Z, Li X, Li Q, Miao Z (2013). "PSMA7 directly interacts with NOD1 and regulates its function". Cellular Physiology and Biochemistry. 31 (6): 952–9. doi:10.1159/000350113. PMID 23839082.
  33. ↑ Cho S, Choi YJ, Kim JM, Jeong ST, Kim JH, Kim SH, Ryu SE (June 2001). "Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7". FEBS Letters. 498 (1): 62–6. doi:10.1016/S0014-5793(01)02499-1. PMID 11389899.
  34. ↑ Feng Y, Longo DL, Ferris DK (January 2001). "Polo-like kinase interacts with proteasomes and regulates their activity". Cell Growth & Differentiation. 12 (1): 29–37. PMID 11205743.

Further reading

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