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KHDRBS3

La KHDRBS3 (pour « KH domain-containing, RNA-binding, signal transduction-associated protein 3 » en anglais) est une protéine codée par le gène KHDRBS3, présent sur le chromosome 8 humain et le chromosome 15 de la souris[1] - [2] - [3].

KHDRBS3
Caractéristiques générales
Nom approuvé KHDRBS3
Synonymes Etle, SALP, SLM-2, SLM2, T-STAR, TSTAR, etoile, KH domain containing, RNA binding, signal transduction associated 3, KH RNA binding domain containing, signal transduction associated 3
PDB 5ELR, 5ELS, 5EMO, 5ELT, 5EL3
Homo sapiens
Locus 8q24.23
Liens accessibles depuis GeneCards et HUGO.
Mus musculus (souris)

Interaction

La KHDRBS3 interagit avec la protéine SIAH1 (en)[4] - [5].

Notes et références
  1. (en) Venables JP, Vernet C, Chew SL, Elliott DJ, Cowmeadow RB, Wu J, Cooke HJ, Artzt K, Eperon IC, « T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis », Hum Mol Genet, vol. 8, no 6,‎ , p. 959–69 (PMID 10332027, DOI 10.1093/hmg/8.6.959).
  2. (en) Lee J, Burr JG, « Salpalpha and Salpbeta, growth-arresting homologs of Sam68 », Gene, vol. 240, no 1,‎ , p. 133–47 (PMID 10564820, DOI 10.1016/S0378-1119(99)00421-7).
  3. (en) « Entrez Gene: KHDRBS3 KH domain containing, RNA binding, signal transduction associated 3 ».
  4. (en) Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M, « Towards a proteome-scale map of the human protein-protein interaction network », Nature, vol. 437, no 7062,‎ , p. 1173–8 (PMID 16189514, DOI 10.1038/nature04209).
  5. (en) Venables JP, Dalgliesh C, Paronetto MP, Skitt L, Thornton JK, Saunders PT, Sette C, Jones KT, Elliott DJ, « SIAH1 targets the alternative splicing factor T-STAR for degradation by the proteasome », Hum. Mol. Genet., vol. 13, no 14,‎ , p. 1525–34 (PMID 15163637, DOI 10.1093/hmg/ddh165).

Bibliographie
  • (en) Di Fruscio M, Chen T, Richard S, « Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1 is a Src substrate during mitosis. », Proc. Natl. Acad. Sci. U.S.A., vol. 96, no 6,‎ , p. 2710–5 (PMID 10077576, PMCID 15834, DOI 10.1073/pnas.96.6.2710)
  • (en) Venables JP, Elliott DJ, Makarova OV, Makarov EM, Cooke HJ, Eperon IC, « RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2beta and affect splicing. », Hum. Mol. Genet., vol. 9, no 5,‎ , p. 685–94 (PMID 10749975, DOI 10.1093/hmg/9.5.685)
  • (en) Stoss O, Olbrich M, Hartmann AM, Konig H, Memmott J, Andreadis A, Stamm S, « The STAR/GSG family protein rSLM-2 regulates the selection of alternative splice sites. », J. Biol. Chem., vol. 276, no 12,‎ , p. 8665–73 (PMID 11118435, DOI 10.1074/jbc.M006851200)
  • (en) Sugimoto Y, Morita R, Amano K, Shah PU, Pascual-Castroviejo I, Khan S, Delgado-Escueta AV, Yamakawa K, « T-STAR gene: fine mapping in the candidate region for childhood absence epilepsy on 8q24 and mutational analysis in patients. », Epilepsy Res., vol. 46, no 2,‎ , p. 139–44 (PMID 11463515, DOI 10.1016/S0920-1211(01)00274-1)
  • (en) Kool J, van Zaane W, van der Eb AJ, Terleth C, « Down-regulation of T-STAR, a growth inhibitory protein, after SV40-mediated immortalization. », Cell Growth Differ., vol. 12, no 11,‎ , p. 535–41 (PMID 11714634)
  • (en) Reddy TR, Suhasini M, Xu W, Yeh LY, Yang JP, Wu J, Artzt K, Wong-Staal F, « A role for KH domain proteins (Sam68-like mammalian proteins and quaking proteins) in the post-transcriptional regulation of HIV replication. », J. Biol. Chem., vol. 277, no 8,‎ , p. 5778–84 (PMID 11741900, DOI 10.1074/jbc.M106836200)
  • (en) CĂ´tĂ© J, Boisvert FM, Boulanger MC, Bedford MT, Richard S, « Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1. », Mol. Biol. Cell, vol. 14, no 1,‎ , p. 274–87 (PMID 12529443, PMCID 140244, DOI 10.1091/mbc.E02-08-0484)
  • (en) Venables JP, Dalgliesh C, Paronetto MP, Skitt L, Thornton JK, Saunders PT, Sette C, Jones KT, Elliott DJ, « SIAH1 targets the alternative splicing factor T-STAR for degradation by the proteasome. », Hum. Mol. Genet., vol. 13, no 14,‎ , p. 1525–34 (PMID 15163637, DOI 10.1093/hmg/ddh165)
  • (en) Cohen CD, Doran PP, Blattner SM, Merkle M, Wang GQ, Schmid H, Mathieson PW, Saleem MA, Henger A, Rastaldi MP, Kretzler M, « Sam68-like mammalian protein 2, identified by digital differential display as expressed by podocytes, is induced in proteinuria and involved in splice site selection of vascular endothelial growth factor. », J. Am. Soc. Nephrol., vol. 16, no 7,‎ , p. 1958–65 (PMID 15901763, DOI 10.1681/ASN.2005020204)
  • (en) Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M, « Towards a proteome-scale map of the human protein-protein interaction network. », Nature, vol. 437, no 7062,‎ , p. 1173–8 (PMID 16189514, DOI 10.1038/nature04209)
  • (en) Zhang L, Guo L, Peng Y, Chen B, « Expression of T-STAR gene is associated with regulation of telomerase activity in human colon cancer cell line HCT-116. », World J. Gastroenterol., vol. 12, no 25,‎ , p. 4056–60 (PMID 16810759)
  • (en) Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M, « Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. », Cell, vol. 127, no 3,‎ , p. 635–48 (PMID 17081983, DOI 10.1016/j.cell.2006.09.026)

Voir aussi

Liens internes
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