Ribosomal protein SA

Ribosomal protein SA
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols RPSA ; 37LRP; 67LR; ICAS; LAMBR; LAMR1; LBP; LBP/p40; LRP; LRP/LR; NEM/1CHD4; SA; lamR; p40
External IDs OMIM: 150370 MGI: 105381 HomoloGene: 68249 ChEMBL: 6119 GeneCards: RPSA Gene
Orthologs
Species Human Mouse
Entrez 3921 16785
Ensembl ENSG00000168028 ENSMUSG00000032518
UniProt P08865 P14206
RefSeq (mRNA) NM_001304288 NM_011029
RefSeq (protein) NP_001291217 NP_035159
Location (UCSC) Chr 3:
39.41 – 39.41 Mb
Chr 9:
120.13 – 120.13 Mb
PubMed search

40S ribosomal protein SA is a Ribosomal protein that in humans is encoded by the RPSA gene.[1][2][3]

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 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 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 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.[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.

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. 1 2 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. 1 2 "Entrez Gene: RPSA ribosomal protein SA".
  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. 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. 1 2 3 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 H (June 2012). "Multiple folding states and disorder of ribosomal protein SA, a membrane receptor for laminin, anticarcinogens, and pathogens". Biochemistry 51 (24): 4807–21. doi:10.1021/bi300335r. PMID 22640394.
  8. 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.
  9. 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.
  10. 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.
  11. 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.
  12. Rao, NC; Barsky, SH; Terranova, VP; Liotta, LA (1983). "Isolation of a tumor cell laminin receptor". Biochem. Biophys. Res. Commun. 111 (3): 804–808. PMID 6301485.
  13. Lesot, H; Kühl, U; Mark, K (1983). "Isolation of a laminin-binding protein from muscle cell membranes". EMBO J. 2 (6): 861–865. PMID 16453457.
  14. 1 2 3 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. PMID 23137297.
  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. 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. 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. 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. 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. PMID 15024383.
  21. Tachibana, H (2011). "Green tea polyphenol sensing". Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. 87 (3): 66–80. PMID 21422740.

Further reading


This article is issued from Wikipedia - version of the Tuesday, May 03, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.