Ribosomal protein SA: Difference between revisions

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{{Infobox_gene}}
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'''40S ribosomal protein SA''' is a [[ribosomal protein]] that in humans is encoded by the ''RPSA'' [[gene]].<ref name="pmid1534510">{{cite journal | vauthors = Satoh K, Narumi K, Sakai T, Abe T, Kikuchi T, Matsushima K, Sindoh S, Motomiya M | title = Cloning of 67-kDa laminin receptor cDNA and gene expression in normal and malignant cell lines of the human lung | journal = Cancer Lett | volume = 62 | issue = 3 | pages = 199–203 | date = Jul 1992 | pmid = 1534510 | pmc =  | doi = 10.1016/0304-3835(92)90096-E }}</ref><ref name="pmid8760291">{{cite journal | vauthors = Jackers P, Minoletti F, Belotti D, Clausse N, Sozzi G, Sobel ME, Castronovo V | title = Isolation from a multigene family of the active human gene of the metastasis-associated multifunctional protein 37LRP/p40 at chromosome 3p21.3 | journal = Oncogene | volume = 13 | issue = 3 | pages = 495–503 | date = Sep 1996 | pmid = 8760291 | pmc = | doi = }}</ref> It also acts as a [[cell surface receptor]], in particular for [[laminin]], and is involved in several pathogenic processes.
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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 =
| image_source =
| PDB =
| Name = Ribosomal protein SA
| HGNCid = 6502
| Symbol = RPSA
| AltSymbols =; 37LRP; 67LR; LAMBR; LAMR1; LRP; p40
| OMIM = 150370
| ECnumber = 
| Homologene = 68249
| MGIid = 105381
| Function = {{GNF_GO|id=GO:0003735 |text = structural constituent of ribosome}} {{GNF_GO|id=GO:0005055 |text = laminin receptor activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005843 |text = cytosolic small ribosomal subunit (sensu Eukaryota)}} {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0015935 |text = small ribosomal subunit}}
| Process = {{GNF_GO|id=GO:0006412 |text = translation}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3921
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_001012321
    | Hs_RefseqmRNA = NM_001012321
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 16785
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_011029
    | Mm_RefseqProtein = NP_035159
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Ribosomal protein SA''', also known as '''RPSA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RPSA ribosomal protein SA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3921| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Laminins]], a family of [[extracellular matrix]] [[glycoproteins]], are the major [[Collagen|noncollagenous]] constituent of [[basement membranes]]. They have been implicated in a wide variety of biological processes including [[cell adhesion]], [[Cellular differentiation|differentiation]], [[Cell migration|migration]], [[Cell signaling|signaling]], [[neurite]] outgrowth and [[metastasis]]. Many of the effects of laminin are mediated through [[List of protein interactions|interactions]] with [[cell surface receptors]]. These receptors include members of the [[integrin]] family, as well as non-integrin laminin-binding proteins. The RPSA gene encodes a multifunctional protein, which is both a ribosomal protein and a high-affinity, non-integrin laminin receptor. This protein has been variously called Ribosomal protein SA; RPSA; LamR; LamR1; 37 kDa Laminin Receptor Precursor; 37LRP; 67 kDa Laminin Receptor; 67LR; 37/67 kDa Laminin Receptor; LRP/LR; LBP/p40; and p40 ribosome-associated protein. Ribosomal protein SA and RPSA are the approved name and symbol.  The [[amino acid]] [[Peptide sequence|sequence]] of RPSA is highly conserved through [[Evolutionary biology|evolution]], suggesting a key [[biological function]]. It has been observed that the level of RPSA [[Transcription (genetics)|transcript]] is higher in [[Large intestine|colon]] [[carcinoma]] [[Tissue (biology)|tissue]] and lung cancer cell lines than their normal counterparts. Also, there is a correlation between the [[Downregulation and upregulation|upregulation]] of this [[peptide|polypeptide]] in cancer cells and their invasive and metastatic [[phenotype]]. Multiple copies of the RPSA gene exist; however, most of them are [[pseudogene]]s thought to have arisen from [[Retroposon|retropositional]] events. Two [[Alternative splicing|alternatively spliced]] transcript variants encoding the same protein have been found for this gene.<ref>{{cite journal|last1=DiGiacomo|first1=Vincent|last2=Meruelo|first2=Daniel|title=Looking into laminin receptor: critical discussion regarding the non-integrin 37/67-kDa laminin receptor/RPSA protein|journal=Biological Reviews|date=May 2016|volume=91|issue=2|pages=288–310|doi=10.1111/brv.12170}}</ref>
{{PBB_Summary
| section_title =
| summary_text = Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Many of the effects of laminin are mediated through interactions with cell surface receptors. These receptors include members of the integrin family, as well as non-integrin laminin-binding proteins. The RPSA gene encodes a high-affinity, non-integrin family, laminin receptor 1. This receptor has been variously called 67 kD laminin receptor, 37 kD laminin receptor precursor (37LRP) and p40 ribosome-associated protein. The amino acid sequence of laminin receptor 1 is highly conserved through evolution, suggesting a key biological function. It has been observed that the level of the laminin receptor transcript is higher in colon carcinoma tissue and lung cancer cell line than their normal counterparts. Also, there is a correlation between the upregulation of this polypeptide in cancer cells and their invasive and metastatic phenotype. Multiple copies of this gene exist, however, most of them are pseudogenes thought to have arisen from retropositional events. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: RPSA ribosomal protein SA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3921| accessdate = }}</ref>
}}


==References==
== Structure and stability ==
{{reflist|2}}
 
==Further reading==
The complementary DNA (cDNA) of the RPSA gene is formed by the assembly of seven exons, six of which correspond to the coding sequence.<ref name="pmid8760291" /> The amino acid sequence of RPSA, deduced from the sequence of its cDNA, includes 295 residues. RPSA can be sub-divided in two main domains: an N-domain (residues 1-209), which corresponds to exons 2-5 of the gene, and a C-domain (residues 210-295), which corresponds to exons 6-7. The N-domain of RPSA is homologous to the ribosomal protein S2 (RPS2) of prokaryotes. It contains a palindromic sequence 173LMWWML178 which is conserved in all metazoans. Its C-domain is highly conserved in vertebrates. The amino acid sequence of RPSA is 98% identical in all mammals. RPSA is a ribosomal protein which has acquired the function of laminin receptor during evolution.<ref>{{cite journal | vauthors = Ardini E, Pesole G, Tagliabue E, Magnifico A, Castronovo V, Sobel ME, Colnaghi MI, Ménard S | title = The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution | journal = Molecular Biology and Evolution | volume = 15 | issue = 8 | pages = 1017–25 | date = August 1998 | pmid = 9718729 | doi=10.1093/oxfordjournals.molbev.a026000}}</ref><ref>{{cite journal | vauthors = Nelson J, McFerran NV, Pivato G, Chambers E, Doherty C, Steele D, Timson DJ | title = The 67 kDa laminin receptor: structure, function and role in disease | journal = Bioscience Reports | volume = 28 | issue = 1 | pages = 33–48 | date = February 2008 | pmid = 18269348 | doi = 10.1042/BSR20070004 }}</ref> The structure of the N-domain of RPSA is similar to those of prokaryotic RPS2.<ref name="pmid18063583">{{cite journal | vauthors = Jamieson KV, Wu J, Hubbard SR, Meruelo D | title = Crystal structure of the human laminin receptor precursor | journal = The Journal of Biological Chemistry | volume = 283 | issue = 6 | pages = 3002–5 | date = February 2008 | pmid = 18063583 | doi = 10.1074/jbc.C700206200 }}</ref> The C-domain is intrinsically disordered in solution. The N-domain is monomeric in solution and unfolds according to a three state equilibrium. The folding intermediate is predominant at 37&nbsp;°C.<ref>{{cite journal|last1=Ould-Abeih|first1=MB|last2=Petit-Topin|first2=I|last3=Zidane|first3=N|last4=Baron|first4=B|last5=Bedouelle|first5=Hugues|title=Multiple folding states and disorder of ribosomal protein SA, a membrane receptor for laminin, anticarcinogens, and pathogens|journal=Biochemistry|date=Jun 2012|volume=51|issue=24|pages=4807–4821|doi=10.1021/bi300335r|pmid=22640394}}</ref>
{{refbegin | 2}}
 
{{PBB_Further_reading
== Interactions ==
| citations =
 
*{{cite journal  | author=Belkin AM, Stepp MA |title=Integrins as receptors for laminins. |journal=Microsc. Res. Tech. |volume=51 |issue= 3 |pages= 280-301 |year= 2000 |pmid= 11054877 |doi= 10.1002/1097-0029(20001101)51:3<280::AID-JEMT7>3.0.CO;2-O }}
Several interactions of RPSA that had originally been discovered by methods of cellular biology, have subsequently been confirmed by using recombinant derivatives and in vitro experiments. The latter have shown that the folded N-domain and disordered C-domain of RPSA have both common and specific functions.<ref name="pmid23137297">{{cite journal|last1=Zidane|first1=N|last2=Ould-Abeih|first2=MB|last3=Petit-Topin|first3=I|last4=Bedouelle|first4=H|title=The folded and disordered domains of human ribosomal protein SA have both idiosyncratic and shared functions as membrane receptors|journal=Biosci. Rep.|date=2012|volume=33|issue=1|pages=113–124|doi=10.1042/BSR20120103|pmid=23137297|pmc=4098866}}</ref>
*{{cite journal | author=Satoh K, Narumi K, Sakai T, ''et al.'' |title=Cloning of 67-kDa laminin receptor cDNA and gene expression in normal and malignant cell lines of the human lung. |journal=Cancer Lett. |volume=62 |issue= 3 |pages= 199-203 |year= 1992 |pmid= 1534510 |doi= }}
* RPSA binds to proteins that are involved in the translation of the genetic code. (i) Yeast two-hybrid screens have shown that RPSA binds to Ribosomal protein S21 of the 40S small ribosomal subunit.<ref>{{cite journal | vauthors = Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–968 | date = Sep 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 }}</ref><ref>{{cite journal | vauthors = Sato M, Saeki Y, Tanaka K, Kaneda Y | title = Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system | journal = Biochem. Biophys. Res. Commun. | volume = 256 | issue = 2 | pages = 385–390 | date = Mar 1999 | pmid = 10079194 | doi = 10.1006/bbrc.1999.0343 }}</ref> (ii) Serial deletions of RPSA have shown that the segment of residues 236-262, included in the C-domain, is involved in the interaction between RPSA and the 40S subunit of ribosome.<ref>{{cite journal|last1=Malygin|first1=AA|last2=Babaylova|first2=ES|last3=Loktev|first3=VB|last4=Karpova|first4=GG|title=A region in the C-terminal domain of ribosomal protein SA required for binding of SA to the human 40S ribosomal subunit|journal=Biochimie|date=2011|volume=93|issue=3|pages=612–617|doi=10.1016/j.biochi.2010.12.005|pmid=21167900}}</ref> (iii) Studies that were based on nuclear magnetic resonance spectroscopy (NMR), have shown that the anticodon binding domain of Lysyl-tRNA synthetase binds directly to the C-domain of RPSA.<ref>{{cite journal|last1=Cho|first1=HY|last2=Ul Mushtaq|first2=A|last3=Lee|first3=JY|last4=Kim|first4=DG|last5=Seok|first5=MS|last6=Jang|first6=M|last7=Han|first7=BW|last8=Kim|first8=S|last9=Jeon|first9=YH|title=Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR|journal=FEBS Lett.|date=2014|volume=588|issue=17|pages=2851–2858|doi=10.1016/j.febslet.2014.06.048|pmid=24983501}}</ref>
*{{cite journal | author=Wewer UM, Liotta LA, Jaye M, ''et al.'' |title=Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 19 |pages= 7137-41 |year= 1986 |pmid= 2429301 |doi= }}
* RPSA was initially identified as a laminin binding protein.<ref>{{cite journal|last1=Rao|first1=NC|last2=Barsky|first2=SH|last3=Terranova|first3=VP|last4=Liotta|first4=LA|title=Isolation of a tumor cell laminin receptor|journal=Biochem. Biophys. Res. Commun.|date=1983|volume=111|issue=3|pages=804–808|pmid=6301485|doi=10.1016/0006-291X(83)91370-0}}</ref><ref>{{cite journal|last1=Lesot|first1=H|last2=Kühl|first2=U|last3=Mark|first3=K|title=Isolation of a laminin-binding protein from muscle cell membranes|journal=EMBO J.|date=1983|volume=2|issue=6|pages=861–865|pmid=16453457|pmc=555201}}</ref> Both recombinant N-domain and C-domain of RPSA bind laminin in vitro, and they bind with similar dissociation constants (300 nM).<ref name="pmid18063583" /><ref name="pmid23137297"/>
*{{cite journal | author=Van den Ouweland AM, Van Duijnhoven HL, Deichmann KA, ''et al.'' |title=Characteristics of a multicopy gene family predominantly consisting of processed pseudogenes. |journal=Nucleic Acids Res. |volume=17 |issue= 10 |pages= 3829-43 |year= 1989 |pmid= 2543954 |doi= }}
* Both RPSA and laminin belong to the heparin/heparan sulfate interactome.<ref>{{cite journal|last1=Ori|first1=A|last2=Wilkinson|first2=MC|last3=Fernig|first3=DG|title=A systems biology approach for the investigation of the heparin/heparan sulfate interactome|journal=J. Biol. Chem.|date=2011|volume=286|issue=22|pages=19892–19904|doi=10.1074/jbc.M111.228114|pmid=21454685|pmc=3103365}}</ref> Heparin binds in vitro to the N-domain of RPSA but not to its C-domain. Moreover, the C-domain of RPSA and heparin compete for binding to laminin, which shows that the highly acidic C-domain of RPSA mimicks heparin (and potentially heparan sulfates) for the binding to laminin.<ref name="pmid23137297" />
*{{cite journal  | author=Yow HK, Wong JM, Chen HS, ''et al.'' |title=Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 17 |pages= 6394-8 |year= 1988 |pmid= 2970639 |doi= }}
* RPSA is a potential cellular receptor for several pathogenic ''Flaviviruses'', including the dengue virus (DENV),<ref>{{cite journal|last1=Thepparit|first1=C|last2=Smith|first2=DR|title=Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor|journal=J. Virol.|date=2004|volume=78|issue=22|pages=12647–12656|pmid=15507651|doi=10.1128/jvi.78.22.12647-12656.2004|pmc=525075}}</ref><ref>{{cite journal|last1=Tio|first1=PH|last2=Jong|first2=WW|last3=Cardosa|first3=MJ|title=Two dimensional VOPBA reveals laminin receptor (LAMR1) interaction with dengue virus serotypes 1, 2 and 3|journal=Virol. J.|date=2005|volume=2|page=25|doi=10.1186/1743-422X-2-25|pmid=15790424|pmc=1079963}}</ref> and ''Alphaviruses'', including the Sindbis virus (SINV).<ref>{{cite journal|last1=Wang|first1=KS|last2=Kuhn|first2=RJ|last3=Strauss|first3=EG|last4=Ou|first4=S|last5=Strauss|first5=JH|title=High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells|journal=J. Virol.|date=1992|volume=66|issue=8|pages=4992–5001|pmid=1385835|pmc=241351}}</ref> The N-domain of RPSA includes a binding site for SINV in vitro.<ref name="pmid18063583" /> The N-domain also includes weak binding sites for recombinant domain 3 (ED3, residues 296-400) from the envelope proteins of two ''Flaviviruses'', West-Nile virus and serotype 2 of DENV. The C-domain includes weak binding sites for domain 3 of the yellow fever virus (YFV) and of serotypes 1 and 2 of DENV. In contrast, domain 3 from the Japanese encephalitis virus does not appear to bind RPSA in vitro.<ref name="pmid23137297" />
*{{cite journal | author=Gehlsen KR, Dillner L, Engvall E, Ruoslahti E |title=The human laminin receptor is a member of the integrin family of cell adhesion receptors. |journal=Science |volume=241 |issue= 4870 |pages= 1228-9 |year= 1988 |pmid= 2970671 |doi=  }}
* RPSA is also a receptor for small molecules. (i) RPSA binds aflatoxin B1 both in vivo and in vitro.<ref>{{cite journal|last1=Zhuang|first1=Z|last2=Huang|first2=Y|last3=Yang|first3=Y|last4=Wang|first4=S|title=Identification of AFB1-interacting proteins and interactions between RPSA and AFB1|journal=J. Hazard. Mater.|date=2016|volume=301|pages=297–303|doi=10.1016/j.jhazmat.2015.08.053|pmid=26372695}}</ref> (ii) RPSA is a receptor for epigallocatechin-gallate (EGCG), which is a major constituent of green tea and has many health related effects.<ref>{{cite journal|last1=Tachibana|first1=H|last2=Koga|first2=K|last3=Fujimura|first3=Y|last4=Yamada|first4=K|title=A receptor for green tea polyphenol EGCG|journal=Nat. Struct. Mol. Biol.|date=2004|volume=11|issue=4|pages=380–381|pmid=15024383|doi=10.1038/nsmb743}}</ref><ref>{{cite journal|last1=Tachibana|first1=H|title=Green tea polyphenol sensing|journal=Proc. Jpn. Acad. Ser. B Phys. Biol. Sci.|date=2011|volume=87|issue=3|pages=66–80|pmid=21422740|doi=10.2183/pjab.87.66|pmc=3066547}}</ref> EGCG binds only to the N-domain of RPSA in vitro, with a dissociation constant of 100 nM, but not to its C-domain.<ref name="pmid23137297" />
*{{cite journal  | author=Selvamurugan N, Eliceiri GL |title=The gene for human E2 small nucleolar RNA resides in an intron of a laminin-binding protein gene. |journal=Genomics |volume=30 |issue= 2 |pages= 400-1 |year= 1996 |pmid= 8586453 |doi= }}
 
*{{cite journal  | author=Vladimirov SN, Ivanov AV, Karpova GG, ''et al.'' |title=Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry. |journal=Eur. J. Biochem. |volume=239 |issue= 1 |pages= 144-9 |year= 1996 |pmid= 8706699 |doi= }}
== References ==
*{{cite journal  | author=Jackers P, Minoletti F, Belotti D, ''et al.'' |title=Isolation from a multigene family of the active human gene of the metastasis-associated multifunctional protein 37LRP/p40 at chromosome 3p21.3. |journal=Oncogene |volume=13 |issue= 3 |pages= 495-503 |year= 1996 |pmid= 8760291 |doi=  }}
{{reflist|33em}}
*{{cite journal  | author=Clausse N, Jackers P, Jarès P, ''et al.'' |title=Identification of the active gene coding for the metastasis-associated 37LRP/p40 multifunctional protein. |journal=DNA Cell Biol. |volume=15 |issue= 12 |pages= 1009-23 |year= 1997 |pmid= 8985115 |doi= }}
 
*{{cite journal | author=Daidone MG, Silvestrini R, Benini E, ''et al.'' |title=Expression of high-affinity 67-kDa laminin receptors in primary breast cancers and metachronous metastatic lesions or contralateral cancers. |journal=Br. J. Cancer |volume=76 |issue= 1 |pages= 52-3 |year= 1997 |pmid= 9218732 |doi= }}
== Further reading ==
*{{cite journal  | author=Kenmochi N, Kawaguchi T, Rozen S, ''et al.'' |title=A map of 75 human ribosomal protein genes. |journal=Genome Res. |volume=8 |issue= 5 |pages= 509-23 |year= 1998 |pmid= 9582194 |doi=  }}
{{refbegin|33em}}
*{{cite journal | author=de Manzoni G, Guglielmi A, Verlato G, ''et al.'' |title=Prognostic significance of 67-kDa laminin receptor expression in advanced gastric cancer. |journal=Oncology |volume=55 |issue= 5 |pages= 456-60 |year= 1998 |pmid= 9732225 |doi=  }}
* {{cite journal | vauthors = Belkin AM, Stepp MA | title = Integrins as receptors for laminins | journal = Microsc. Res. Tech. | volume = 51 | issue = 3 | pages = 280–301 | year = 2000 | pmid = 11054877 | doi = 10.1002/1097-0029(20001101)51:3<280::AID-JEMT7>3.0.CO;2-O }}
*{{cite journal | author=Sato M, Saeki Y, Tanaka K, Kaneda Y |title=Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system. |journal=Biochem. Biophys. Res. Commun. |volume=256 |issue= 2 |pages= 385-90 |year= 1999 |pmid= 10079194 |doi= 10.1006/bbrc.1999.0343 }}
* {{cite journal | vauthors = Wewer UM, Liotta LA, Jaye M, Ricca GA, Drohan WN, Claysmith AP, Rao CN, Wirth P, Coligan JE, Albrechtsen R | title = Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 83 | issue = 19 | pages = 7137–7141 | year = 1986 | pmid = 2429301 | pmc = 386670 | doi = 10.1073/pnas.83.19.7137 }}
*{{cite journal | author=Canfield SM, Khakoo AY |title=The nonintegrin laminin binding protein (p67 LBP) is expressed on a subset of activated human T lymphocytes and, together with the integrin very late activation antigen-6, mediates avid cellular adherence to laminin. |journal=J. Immunol. |volume=163 |issue= 6 |pages= 3430-40 |year= 1999 |pmid= 10477615 |doi= }}
* {{cite journal | vauthors = Van den Ouweland AM, Van Duijnhoven HL, Deichmann KA, Van Groningen JJ, de Leij L, Van de Ven WJ | title = Characteristics of a multicopy gene family predominantly consisting of processed pseudogenes | journal = Nucleic Acids Res. | volume = 17 | issue = 10 | pages = 3829–3843 | year = 1989 | pmid = 2543954 | pmc = 317862 | doi = 10.1093/nar/17.10.3829 }}
*{{cite journal | author=Donaldson EA, McKenna DJ, McMullen CB, ''et al.'' |title=The expression of membrane-associated 67-kDa laminin receptor (67LR) is modulated in vitro by cell-contact inhibition. |journal=Mol. Cell Biol. Res. Commun. |volume=3 |issue= 1 |pages= 53-9 |year= 2000 |pmid= 10683318 |doi= 10.1006/mcbr.2000.0191 }}
* {{cite journal | vauthors = Yow HK, Wong JM, Chen HS, Lee CG, Davis S, Steele GD, Chen LB | title = Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 85 | issue = 17 | pages = 6394–6398 | year = 1988 | pmid = 2970639 | pmc = 281978 | doi = 10.1073/pnas.85.17.6394 | url = http://ntur.lib.ntu.edu.tw//bitstream/246246/127028/1/Laminin%2BReceptor.pdf }}
*{{cite journal  | author=Pedraza C, Geberhiwot T, Ingerpuu S, ''et al.'' |title=Monocytic cells synthesize, adhere to, and migrate on laminin-8 (alpha 4 beta 1 gamma 1). |journal=J. Immunol. |volume=165 |issue= 10 |pages= 5831-8 |year= 2000 |pmid= 11067943 |doi= }}
* {{cite journal | vauthors = Selvamurugan N, Eliceiri GL | title = The gene for human E2 small nucleolar RNA resides in an intron of a laminin-binding protein gene | journal = Genomics | volume = 30 | issue = 2 | pages = 400–1 | year = 1996 | pmid = 8586453 | doi =  }}
*{{cite journal | author=Vande Broek I, Vanderkerken K, De Greef C, ''et al.'' |title=Laminin-1-induced migration of multiple myeloma cells involves the high-affinity 67 kD laminin receptor. |journal=Br. J. Cancer |volume=85 |issue= 9 |pages= 1387-95 |year= 2001 |pmid= 11720479 |doi= 10.1054/bjoc.2001.2078 }}
* {{cite journal | vauthors = Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, Wittmann-Liebold B, Otto A | title = Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry | journal = Eur. J. Biochem. | volume = 239 | issue = 1 | pages = 144–149 | year = 1996 | pmid = 8706699 | doi = 10.1111/j.1432-1033.1996.0144u.x }}
*{{cite journal | author=Waltregny D, de Leval L, Coppens L, ''et al.'' |title=Detection of the 67-kD laminin receptor in prostate cancer biopsies as a predictor of recurrence after radical prostatectomy. |journal=Eur. Urol. |volume=40 |issue= 5 |pages= 495-503 |year= 2002 |pmid= 11752855 |doi= }}
* {{cite journal | vauthors = Clausse N, Jackers P, Jarès P, Joris B, Sobel ME, Castronovo V | title = Identification of the active gene coding for the metastasis-associated 37LRP/p40 multifunctional protein | journal = DNA Cell Biol. | volume = 15 | issue = 12 | pages = 1009–1023 | year = 1997 | pmid = 8985115 | doi = 10.1089/dna.1996.15.1009 }}
}}
* {{cite journal | vauthors = Daidone MG, Silvestrini R, Benini E, Grigioni WF, D'Errico A | title = Expression of high-affinity 67-kDa laminin receptors in primary breast cancers and metachronous metastatic lesions or contralateral cancers | journal = Br. J. Cancer | volume = 76 | issue = 1 | pages = 52–3 | year = 1997 | pmid = 9218732 | pmc = 2223804 | doi = 10.1038/bjc.1997.335 }}
* {{cite journal | vauthors = Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC | title = A map of 75 human ribosomal protein genes | journal = Genome Res. | volume = 8 | issue = 5 | pages = 509–23 | year = 1998 | pmid = 9582194 | doi = 10.1101/gr.8.5.509 }}
* {{cite journal | vauthors = de Manzoni G, Guglielmi A, Verlato G, Tomezzoli A, Pelosi G, Schiavon I, Cordiano C | title = Prognostic significance of 67-kDa laminin receptor expression in advanced gastric cancer | journal = Oncology | volume = 55 | issue = 5 | pages = 456–460 | year = 1998 | pmid = 9732225 | doi = 10.1159/000011895 }}
* {{cite journal | vauthors = Sato M, Saeki Y, Tanaka K, Kaneda Y | title = Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system | journal = Biochem. Biophys. Res. Commun. | volume = 256 | issue = 2 | pages = 385–390 | year = 1999 | pmid = 10079194 | doi = 10.1006/bbrc.1999.0343 }}
* {{cite journal | vauthors = Canfield SM, Khakoo AY | title = The nonintegrin laminin binding protein (p67 LBP) is expressed on a subset of activated human T lymphocytes and, together with the integrin very late activation antigen-6, mediates avid cellular adherence to laminin | journal = J. Immunol. | volume = 163 | issue = 6 | pages = 3430–40 | year = 1999 | pmid = 10477615 | doi =  }}
* {{cite journal | vauthors = Donaldson EA, McKenna DJ, McMullen CB, Scott WN, Stitt AW, Nelson J | title = The expression of membrane-associated 67-kDa laminin receptor (67LR) is modulated in vitro by cell-contact inhibition | journal = Mol. Cell Biol. Res. Commun. | volume = 3 | issue = 1 | pages = 53–59 | year = 2000 | pmid = 10683318 | doi = 10.1006/mcbr.2000.0191 }}
* {{cite journal | vauthors = Pedraza C, Geberhiwot T, Ingerpuu S, Assefa D, Wondimu Z, Kortesmaa J, Tryggvason K, Virtanen I, Patarroyo M | title = Monocytic cells synthesize, adhere to, and migrate on laminin-8 (alpha 4 beta 1 gamma 1) | journal = J. Immunol. | volume = 165 | issue = 10 | pages = 5831–8 | year = 2000 | pmid = 11067943 | doi = 10.4049/jimmunol.165.10.5831 }}
* {{cite journal | vauthors = Vande Broek I, Vanderkerken K, De Greef C, Asosingh K, Straetmans N, Van Camp B, Van Riet I | title = Laminin-1-induced migration of multiple myeloma cells involves the high-affinity 67 kD laminin receptor | journal = Br. J. Cancer | volume = 85 | issue = 9 | pages = 1387–1395 | year = 2001 | pmid = 11720479 | pmc = 2375239 | doi = 10.1054/bjoc.2001.2078 }}
* {{cite journal | vauthors = Waltregny D, de Leval L, Coppens L, Youssef E, de Leval J, Castronovo V | title = Detection of the 67-kD laminin receptor in prostate cancer biopsies as a predictor of recurrence after radical prostatectomy | journal = Eur. Urol. | volume = 40 | issue = 5 | pages = 495–503 | year = 2002 | pmid = 11752855 | doi = 10.1159/000049825 }}
{{refend}}
{{refend}}


{{protein-stub}}
{{GeneticTranslation}}
{{Ribosome subunits}}
 
[[Category:Ribosomal proteins]]
[[Category:Transmembrane receptors]]

Latest revision as of 14:28, 4 November 2018

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40S ribosomal protein SA is a ribosomal protein that in humans is encoded by the RPSA gene.[1][2] It also acts as a cell surface receptor, in particular for laminin, and is involved in several pathogenic processes.

Function

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Many of the effects of laminin are mediated through interactions with cell surface receptors. These receptors include members of the integrin family, as well as non-integrin laminin-binding proteins. The RPSA gene encodes a multifunctional protein, which is both a ribosomal protein and a high-affinity, non-integrin laminin receptor. This protein has been variously called Ribosomal protein SA; RPSA; LamR; LamR1; 37 kDa Laminin Receptor Precursor; 37LRP; 67 kDa Laminin Receptor; 67LR; 37/67 kDa Laminin Receptor; LRP/LR; LBP/p40; and p40 ribosome-associated protein. Ribosomal protein SA and RPSA are the approved name and symbol. The amino acid sequence of RPSA is highly conserved through evolution, suggesting a key biological function. It has been observed that the level of RPSA transcript is higher in colon carcinoma tissue and lung cancer cell lines than their normal counterparts. Also, there is a correlation between the upregulation of this polypeptide in cancer cells and their invasive and metastatic phenotype. Multiple copies of the RPSA gene exist; however, most of them are pseudogenes thought to have arisen from retropositional events. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.[3]

Structure and stability

The complementary DNA (cDNA) of the RPSA gene is formed by the assembly of seven exons, six of which correspond to the coding sequence.[2] The amino acid sequence of RPSA, deduced from the sequence of its cDNA, includes 295 residues. RPSA can be sub-divided in two main domains: an N-domain (residues 1-209), which corresponds to exons 2-5 of the gene, and a C-domain (residues 210-295), which corresponds to exons 6-7. The N-domain of RPSA is homologous to the ribosomal protein S2 (RPS2) of prokaryotes. It contains a palindromic sequence 173LMWWML178 which is conserved in all metazoans. Its C-domain is highly conserved in vertebrates. The amino acid sequence of RPSA is 98% identical in all mammals. RPSA is a ribosomal protein which has acquired the function of laminin receptor during evolution.[4][5] The structure of the N-domain of RPSA is similar to those of prokaryotic RPS2.[6] The C-domain is intrinsically disordered in solution. The N-domain is monomeric in solution and unfolds according to a three state equilibrium. The folding intermediate is predominant at 37 °C.[7]

Interactions

Several interactions of RPSA that had originally been discovered by methods of cellular biology, have subsequently been confirmed by using recombinant derivatives and in vitro experiments. The latter have shown that the folded N-domain and disordered C-domain of RPSA have both common and specific functions.[8]

  • RPSA binds to proteins that are involved in the translation of the genetic code. (i) Yeast two-hybrid screens have shown that RPSA binds to Ribosomal protein S21 of the 40S small ribosomal subunit.[9][10] (ii) Serial deletions of RPSA have shown that the segment of residues 236-262, included in the C-domain, is involved in the interaction between RPSA and the 40S subunit of ribosome.[11] (iii) Studies that were based on nuclear magnetic resonance spectroscopy (NMR), have shown that the anticodon binding domain of Lysyl-tRNA synthetase binds directly to the C-domain of RPSA.[12]
  • RPSA was initially identified as a laminin binding protein.[13][14] Both recombinant N-domain and C-domain of RPSA bind laminin in vitro, and they bind with similar dissociation constants (300 nM).[6][8]
  • Both RPSA and laminin belong to the heparin/heparan sulfate interactome.[15] Heparin binds in vitro to the N-domain of RPSA but not to its C-domain. Moreover, the C-domain of RPSA and heparin compete for binding to laminin, which shows that the highly acidic C-domain of RPSA mimicks heparin (and potentially heparan sulfates) for the binding to laminin.[8]
  • RPSA is a potential cellular receptor for several pathogenic Flaviviruses, including the dengue virus (DENV),[16][17] and Alphaviruses, including the Sindbis virus (SINV).[18] The N-domain of RPSA includes a binding site for SINV in vitro.[6] The N-domain also includes weak binding sites for recombinant domain 3 (ED3, residues 296-400) from the envelope proteins of two Flaviviruses, West-Nile virus and serotype 2 of DENV. The C-domain includes weak binding sites for domain 3 of the yellow fever virus (YFV) and of serotypes 1 and 2 of DENV. In contrast, domain 3 from the Japanese encephalitis virus does not appear to bind RPSA in vitro.[8]
  • RPSA is also a receptor for small molecules. (i) RPSA binds aflatoxin B1 both in vivo and in vitro.[19] (ii) RPSA is a receptor for epigallocatechin-gallate (EGCG), which is a major constituent of green tea and has many health related effects.[20][21] EGCG binds only to the N-domain of RPSA in vitro, with a dissociation constant of 100 nM, but not to its C-domain.[8]

References

  1. ↑ Satoh K, Narumi K, Sakai T, Abe T, Kikuchi T, Matsushima K, Sindoh S, Motomiya M (Jul 1992). "Cloning of 67-kDa laminin receptor cDNA and gene expression in normal and malignant cell lines of the human lung". Cancer Lett. 62 (3): 199–203. doi:10.1016/0304-3835(92)90096-E. PMID 1534510.
  2. ↑ 2.0 2.1 Jackers P, Minoletti F, Belotti D, Clausse N, Sozzi G, Sobel ME, Castronovo V (Sep 1996). "Isolation from a multigene family of the active human gene of the metastasis-associated multifunctional protein 37LRP/p40 at chromosome 3p21.3". Oncogene. 13 (3): 495–503. PMID 8760291.
  3. ↑ DiGiacomo, Vincent; Meruelo, Daniel (May 2016). "Looking into laminin receptor: critical discussion regarding the non-integrin 37/67-kDa laminin receptor/RPSA protein". Biological Reviews. 91 (2): 288–310. doi:10.1111/brv.12170.
  4. ↑ Ardini E, Pesole G, Tagliabue E, Magnifico A, Castronovo V, Sobel ME, Colnaghi MI, Ménard S (August 1998). "The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution". Molecular Biology and Evolution. 15 (8): 1017–25. doi:10.1093/oxfordjournals.molbev.a026000. PMID 9718729.
  5. ↑ Nelson J, McFerran NV, Pivato G, Chambers E, Doherty C, Steele D, Timson DJ (February 2008). "The 67 kDa laminin receptor: structure, function and role in disease". Bioscience Reports. 28 (1): 33–48. doi:10.1042/BSR20070004. PMID 18269348.
  6. ↑ 6.0 6.1 6.2 Jamieson KV, Wu J, Hubbard SR, Meruelo D (February 2008). "Crystal structure of the human laminin receptor precursor". The Journal of Biological Chemistry. 283 (6): 3002–5. doi:10.1074/jbc.C700206200. PMID 18063583.
  7. ↑ Ould-Abeih, MB; Petit-Topin, I; Zidane, N; Baron, B; Bedouelle, Hugues (Jun 2012). "Multiple folding states and disorder of ribosomal protein SA, a membrane receptor for laminin, anticarcinogens, and pathogens". Biochemistry. 51 (24): 4807–4821. doi:10.1021/bi300335r. PMID 22640394.
  8. ↑ 8.0 8.1 8.2 8.3 8.4 Zidane, N; Ould-Abeih, MB; Petit-Topin, I; Bedouelle, H (2012). "The folded and disordered domains of human ribosomal protein SA have both idiosyncratic and shared functions as membrane receptors". Biosci. Rep. 33 (1): 113–124. doi:10.1042/BSR20120103. PMC 4098866. PMID 23137297.
  9. ↑ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–968. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
  10. ↑ Sato M, Saeki Y, Tanaka K, Kaneda Y (Mar 1999). "Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system". Biochem. Biophys. Res. Commun. 256 (2): 385–390. doi:10.1006/bbrc.1999.0343. PMID 10079194.
  11. ↑ Malygin, AA; Babaylova, ES; Loktev, VB; Karpova, GG (2011). "A region in the C-terminal domain of ribosomal protein SA required for binding of SA to the human 40S ribosomal subunit". Biochimie. 93 (3): 612–617. doi:10.1016/j.biochi.2010.12.005. PMID 21167900.
  12. ↑ Cho, HY; Ul Mushtaq, A; Lee, JY; Kim, DG; Seok, MS; Jang, M; Han, BW; Kim, S; Jeon, YH (2014). "Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR". FEBS Lett. 588 (17): 2851–2858. doi:10.1016/j.febslet.2014.06.048. PMID 24983501.
  13. ↑ Rao, NC; Barsky, SH; Terranova, VP; Liotta, LA (1983). "Isolation of a tumor cell laminin receptor". Biochem. Biophys. Res. Commun. 111 (3): 804–808. doi:10.1016/0006-291X(83)91370-0. PMID 6301485.
  14. ↑ Lesot, H; Kühl, U; Mark, K (1983). "Isolation of a laminin-binding protein from muscle cell membranes". EMBO J. 2 (6): 861–865. PMC 555201. PMID 16453457.
  15. ↑ Ori, A; Wilkinson, MC; Fernig, DG (2011). "A systems biology approach for the investigation of the heparin/heparan sulfate interactome". J. Biol. Chem. 286 (22): 19892–19904. doi:10.1074/jbc.M111.228114. PMC 3103365. PMID 21454685.
  16. ↑ Thepparit, C; Smith, DR (2004). "Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor". J. Virol. 78 (22): 12647–12656. doi:10.1128/jvi.78.22.12647-12656.2004. PMC 525075. PMID 15507651.
  17. ↑ Tio, PH; Jong, WW; Cardosa, MJ (2005). "Two dimensional VOPBA reveals laminin receptor (LAMR1) interaction with dengue virus serotypes 1, 2 and 3". Virol. J. 2: 25. doi:10.1186/1743-422X-2-25. PMC 1079963. PMID 15790424.
  18. ↑ Wang, KS; Kuhn, RJ; Strauss, EG; Ou, S; Strauss, JH (1992). "High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells". J. Virol. 66 (8): 4992–5001. PMC 241351. PMID 1385835.
  19. ↑ Zhuang, Z; Huang, Y; Yang, Y; Wang, S (2016). "Identification of AFB1-interacting proteins and interactions between RPSA and AFB1". J. Hazard. Mater. 301: 297–303. doi:10.1016/j.jhazmat.2015.08.053. PMID 26372695.
  20. ↑ Tachibana, H; Koga, K; Fujimura, Y; Yamada, K (2004). "A receptor for green tea polyphenol EGCG". Nat. Struct. Mol. Biol. 11 (4): 380–381. doi:10.1038/nsmb743. PMID 15024383.
  21. ↑ Tachibana, H (2011). "Green tea polyphenol sensing". Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. 87 (3): 66–80. doi:10.2183/pjab.87.66. PMC 3066547. PMID 21422740.

Further reading

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