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Ribosomal protein SA

From Wikipedia, the free encyclopedia
RPSA
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRPSA, 37LRP, 67LR, ICAS, LAMBR, LAMR1, LBP, LBP/p40, LRP, LRP/LR, NEM/1CHD4, SA, lamR, p40, Ribosomal protein SA
External IDsOMIM: 150370; MGI: 105381; HomoloGene: 68249; GeneCards: RPSA; OMA:RPSA - orthologs
Orthologs
SpeciesHumanMouse
Entrez

3921

16785

Ensembl

ENSG00000168028

ENSMUSG00000032518

UniProt

P08865

P14206

RefSeq (mRNA)

NM_002295
NM_001304288

NM_011029

RefSeq (protein)

NP_001291217
NP_002286

NP_035159

Location (UCSC)Chr 3: 39.41 – 39.41 MbChr 9: 119.96 – 119.96 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

40S ribosomal protein SA is a ribosomal protein that in humans is encoded by the RPSA gene.[5][6] It also acts as a cell surface receptor, in particular for laminin, and is involved in several pathogenic processes.

Function

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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.[7]

Structure and stability

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The complementary DNA (cDNA) of the RPSA gene is formed by the assembly of seven exons, six of which correspond to the coding sequence.[6] 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.[8][9] The structure of the N-domain of RPSA is similar to those of prokaryotic RPS2.[10] 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.[11]

Interactions

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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.[12]

  • 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.[13][14] (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.[15] (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.[16]
  • RPSA was initially identified as a laminin binding protein.[17][18] Both recombinant N-domain and C-domain of RPSA bind laminin in vitro, and they bind with similar dissociation constants (300 nM).[10][12]
  • Both RPSA and laminin belong to the heparin/heparan sulfate interactome.[19] 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.[12]
  • RPSA is a potential cellular receptor for several pathogenic Flaviviruses, including the dengue virus (DENV),[20][21] and Alphaviruses, including the Sindbis virus (SINV).[22] The N-domain of RPSA includes a binding site for SINV in vitro.[10] 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.[12]
  • RPSA is also a receptor for small molecules. (i) RPSA binds aflatoxin B1 both in vivo and in vitro.[23] (ii) RPSA is a receptor for epigallocatechin-gallate (EGCG), which is a major constituent of green tea and has many health related effects.[24][25] EGCG binds only to the N-domain of RPSA in vitro, with a dissociation constant of 100 nM, but not to its C-domain.[12]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000168028 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032518 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ a b 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.
  7. ^ 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. PMC 5249262. PMID 25630983.
  8. ^ 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.
  9. ^ 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.
  10. ^ a b c 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.
  11. ^ 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.
  12. ^ a b c d e 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.
  13. ^ 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. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
  14. ^ 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.
  15. ^ 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.
  16. ^ 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. S2CID 36128866.
  17. ^ 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.
  18. ^ Lesot, H; Kühl, U; Mark, K (1983). "Isolation of a laminin-binding protein from muscle cell membranes". EMBO J. 2 (6): 861–865. doi:10.1002/j.1460-2075.1983.tb01514.x. PMC 555201. PMID 16453457.
  19. ^ 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.
  20. ^ 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.
  21. ^ 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.
  22. ^ 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. doi:10.1128/JVI.66.8.4992-5001.1992. PMC 241351. PMID 1385835.
  23. ^ 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.
  24. ^ 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. S2CID 27868813.
  25. ^ Tachibana, H (2011). "Green tea polyphenol sensing". Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. 87 (3): 66–80. Bibcode:2011PJAB...87...66T. doi:10.2183/pjab.87.66. PMC 3066547. PMID 21422740.

Further reading

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