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Volumn 5, Issue , 2004, Pages

Sam68 exerts separable effects on cell cycle progression and apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; CELL PROTEIN; CYCLIN D1; CYCLIN E; DIMETHYL SULFOXIDE; DOXYCYCLINE; NOCODAZOLE; PROTEIN SAM68; RETINOBLASTOMA PROTEIN; RNA; RNA BINDING PROTEIN; TRICHOSTATIN A;

EID: 2342547025     PISSN: 14712121     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2121-5-5     Document Type: Article
Times cited : (66)

References (28)
  • 1
    • 0028329195 scopus 로고
    • An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis
    • Taylor SJ, Shalloway D: An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis. Nature 1994, 368:867-871.
    • (1994) Nature , vol.368 , pp. 867-871
    • Taylor, S.J.1    Shalloway, D.2
  • 3
    • 0034717290 scopus 로고    scopus 로고
    • Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains
    • Bedford MT, Frankel A, Yaffe MB, Clarke S, Leder P, Richard S: Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains. J Biol Chem 2000, 275:16030-16036.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16030-16036
    • Bedford, M.T.1    Frankel, A.2    Yaffe, M.B.3    Clarke, S.4    Leder, P.5    Richard, S.6
  • 5
    • 0028947757 scopus 로고
    • Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family kinases, Grb2 and phospholipase C gamma-1
    • Richard S, Yu D, Blumer KJ, Hausladen D, Olszowy MW, Connelly PA, Shaw AS: Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family kinases, Grb2 and phospholipase C gamma-1. Mol Cell Biol 1995, 15:186-197.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 186-197
    • Richard, S.1    Yu, D.2    Blumer, K.J.3    Hausladen, D.4    Olszowy, M.W.5    Connelly, P.A.6    Shaw, A.S.7
  • 6
    • 0028945960 scopus 로고
    • Functional interaction between c-Src and its mitotic target, Sam 68
    • Taylor SJ, Anafi M, Pawson T, Shalloway D: Functional interaction between c-Src and its mitotic target, Sam 68. J Biol Chem 1995, 270:10120-10124.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10120-10124
    • Taylor, S.J.1    Anafi, M.2    Pawson, T.3    Shalloway, D.4
  • 8
    • 0030879866 scopus 로고    scopus 로고
    • Self association of the single-KH-domain family members Sam68, GRP33, GLD-1, and Qk1: Role of the KH domain
    • Chen T, Damaj BB, Herrera C, Lasko P, Richard S: Self association of the single-KH-domain family members Sam68, GRP33, GLD-1, and Qk1: role of the KH domain. Mol Cell Biol 1997, 17:5707-5718.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 5707-5718
    • Chen, T.1    Damaj, B.B.2    Herrera, C.3    Lasko, P.4    Richard, S.5
  • 9
    • 0030882332 scopus 로고    scopus 로고
    • Specificity and determinants of Sam68 RNA binding. Implications for the biological function of K homology domains
    • Lin Q, Taylor SJ, Shalloway D: Specificity and determinants of Sam68 RNA binding. Implications for the biological function of K homology domains. J Biol Chem 1997, 272:27274-27280.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27274-27280
    • Lin, Q.1    Taylor, S.J.2    Shalloway, D.3
  • 10
    • 0031858861 scopus 로고    scopus 로고
    • Structure-function analysis of Qk1: A lethal point mutation in mouse quaking prevents homodimerization
    • Chen T, Richard S: Structure-function analysis of Qk1: a lethal point mutation in mouse quaking prevents homodimerization. Mol Cell Biol 1998, 18:4863-4871.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 4863-4871
    • Chen, T.1    Richard, S.2
  • 11
    • 0032514925 scopus 로고    scopus 로고
    • The identification of two Drosophila K homology domain proteins. Kep1 and SAM are members of the Sam68 family of GSG domain proteins
    • Di Fruscio M, Chen T, Bonyadi S, Lasko P, Richard S: The identification of two Drosophila K homology domain proteins. Kep1 and SAM are members of the Sam68 family of GSG domain proteins. J Biol Chem 1998, 273:30122-30130.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30122-30130
    • Di Fruscio, M.1    Chen, T.2    Bonyadi, S.3    Lasko, P.4    Richard, S.5
  • 12
    • 0032980047 scopus 로고    scopus 로고
    • Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1 is a Src substrate during mitosis
    • 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 USA 1999, 96:2710-2715.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2710-2715
    • Di Fruscio, M.1    Chen, T.2    Richard, S.3
  • 13
    • 0032844207 scopus 로고    scopus 로고
    • A role for the GSG domain in localizing Sam68 to novel nuclear structures in cancer cells
    • Chen T, Boisvert F, Bazett-Jones D, Richard S: A role for the GSG domain in localizing Sam68 to novel nuclear structures in cancer cells. Mol Biol Cell 1999, 10:3015-3033.
    • (1999) Mol. Biol Cell , vol.10 , pp. 3015-3033
    • Chen, T.1    Boisvert, F.2    Bazett-Jones, D.3    Richard, S.4
  • 15
    • 0031777384 scopus 로고    scopus 로고
    • The use of antibodies to the polypyrimidine tract binding protein (PTB) to analyze the protein components that assemble on alternatively spliced pre-mRNAs that use distant branch points
    • Grossman JS, Meyer MI, Wang YC, Mulligan GJ, Kobayashi R, Helfman DM: The use of antibodies to the polypyrimidine tract binding protein (PTB) to analyze the protein components that assemble on alternatively spliced pre-mRNAs that use distant branch points. RNA 1998, 4:613-625.
    • (1998) RNA , vol.4 , pp. 613-625
    • Grossman, J.S.1    Meyer, M.I.2    Wang, Y.C.3    Mulligan, G.J.4    Kobayashi, R.5    Helfman, D.M.6
  • 16
    • 0032739144 scopus 로고    scopus 로고
    • The interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn)
    • Hartmann AM, Nayler O, Schwaiger FW, Obermeier A, Stamm S: The interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn). Mol Biol Cell 1999, 10:3909-3926.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3909-3926
    • Hartmann, A.M.1    Nayler, O.2    Schwaiger, F.W.3    Obermeier, A.4    Stamm, S.5
  • 17
    • 0037069651 scopus 로고    scopus 로고
    • Signal dependent regulation of splicing via phosphorylation of Sam68
    • Matter N, Herrlich P, Konig H: Signal dependent regulation of splicing via phosphorylation of Sam68. Nature 2002, 420:691-695.
    • (2002) Nature , vol.420 , pp. 691-695
    • Matter, N.1    Herrlich, P.2    Konig, H.3
  • 18
    • 0036311558 scopus 로고    scopus 로고
    • Direct participation of Sam68, the 68-Kilodalton Src-associated protein in mitosis, in the CRM1-mediated Rev nuclear export pathway
    • Li J, Liu Y, Kim BO, He JH: Direct participation of Sam68, the 68-Kilodalton Src-associated protein in mitosis, in the CRM1-mediated Rev nuclear export pathway. J Virol 2002, 76:8374-8382.
    • (2002) J. Virol. , vol.76 , pp. 8374-8382
    • Li, J.1    Liu, Y.2    Kim, B.O.3    He, J.H.4
  • 21
    • 0344321888 scopus 로고    scopus 로고
    • Physical and functional interaction between the transcriptional cofactor CBP and the KH domain protein Sam68
    • Hong W, Resnick RJ, Rakowski C, Shalloway D, Taylor SJ, Blobel GA: Physical and functional interaction between the transcriptional cofactor CBP and the KH domain protein Sam68. Mol Cancer Res 2002, 1:48-55.
    • (2002) Mol. Cancer Res. , vol.1 , pp. 48-55
    • Hong, W.1    Resnick, R.J.2    Rakowski, C.3    Shalloway, D.4    Taylor, S.J.5    Blobel, G.A.6
  • 22
    • 0037126394 scopus 로고    scopus 로고
    • Functional interaction of Sam68 and heterogeneous nuclear ribonucleoprotein K
    • Yang JP, Reddy TR, Truong KT, Suhasini M, Wong-Staal F: Functional interaction of Sam68 and heterogeneous nuclear ribonucleoprotein K. Oncogene 2002, 21:7187-7194.
    • (2002) Oncogene , vol.21 , pp. 7187-7194
    • Yang, J.P.1    Reddy, T.R.2    Truong, K.T.3    Suhasini, M.4    Wong-Staal, F.5
  • 23
    • 0028963413 scopus 로고
    • p62 association with RNA is regulated by tyrosine phosphorylation
    • Wang LL, Richard S, Shaw AS: p62 association with RNA is regulated by tyrosine phosphorylation. J Biol Chem 1995, 270:2010-2013.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2010-2013
    • Wang, L.L.1    Richard, S.2    Shaw, A.S.3
  • 24
    • 0034704172 scopus 로고    scopus 로고
    • Neoplastic transformation and tumorigenesis associated with Sam68 protein deficiency in cultured murine fibroblasts
    • Liu K, Li L, Nisson PE, Gruber C, Jessee J, Cohen SN: Neoplastic transformation and tumorigenesis associated with Sam68 protein deficiency in cultured murine fibroblasts. J Biol Chem 2000, 275:40195-40201.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40195-40201
    • Liu, K.1    Li, L.2    Nisson, P.E.3    Gruber, C.4    Jessee, J.5    Cohen, S.N.6
  • 25
    • 0037077711 scopus 로고    scopus 로고
    • Retardation of the G2-M phase progression on gene disruption of RNA binding protein Sam68 in the DT40 cell line
    • Li QH, Haga I, Shimizu T, Itoh M, Kurosaki T, Fujisawa J: Retardation of the G2-M phase progression on gene disruption of RNA binding protein Sam68 in the DT40 cell line. FEBS Lett 2002, 525:145-150.
    • (2002) FEBS Lett. , vol.525 , pp. 145-150
    • Li, Q.H.1    Haga, I.2    Shimizu, T.3    Itoh, M.4    Kurosaki, T.5    Fujisawa, J.6
  • 26
    • 0031030580 scopus 로고    scopus 로고
    • A role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domain
    • Barlat I, Maurier F, Duchesne M, Guitard E, Tocque B, Schweighoffer F: A role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domain. J Biol Chem 1997, 272:3129-3132.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3129-3132
    • Barlat, I.1    Maurier, F.2    Duchesne, M.3    Guitard, E.4    Tocque, B.5    Schweighoffer, F.6
  • 27
    • 0037115819 scopus 로고    scopus 로고
    • Identification of cellular mRNA targets for RNA binding protein Sam68
    • Itoh M, Haga I, Li QH, Fujisawa J: Identification of cellular mRNA targets for RNA binding protein Sam68. Nuc Acids Res 2002, 30:5452-5464.
    • (2002) Nuc. Acids Res. , vol.30 , pp. 5452-5464
    • Itoh, M.1    Haga, I.2    Li, Q.H.3    Fujisawa, J.4
  • 28
    • 0029015430 scopus 로고
    • Mutations in gld-1, a female germ cell-specific tumor suppressor gene in C. elegans, affect a conserved domain also found in Src-associated Sam68
    • Jones AR, Schedl T: Mutations in gld-1, a female germ cell-specific tumor suppressor gene in C. elegans, affect a conserved domain also found in Src-associated Sam68. Genes Dev 1995, 9:1491-504.
    • (1995) Genes Dev. , vol.9 , pp. 1491-1504
    • Jones, A.R.1    Schedl, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.