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Volumn 23, Issue 12, 2003, Pages 4139-4149

Regulation and substrate specificity of the SR protein kinase Clk/Sty

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE; SR PROTEIN KINASE CLK; SR PROTEIN KINASE STY; UNCLASSIFIED DRUG;

EID: 0038656410     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.12.4139-4149.2003     Document Type: Article
Times cited : (52)

References (65)
  • 1
    • 0026011116 scopus 로고
    • A mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulators
    • Ben-David, Y., K. Letwin, L. Tannock, A. Bernstein, and T. Pawson. 1991. A mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulators. EMBO J. 10:317-325.
    • (1991) EMBO J. , vol.10 , pp. 317-325
    • Ben-David, Y.1    Letwin, K.2    Tannock, L.3    Bernstein, A.4    Pawson, T.5
  • 2
    • 0031929940 scopus 로고    scopus 로고
    • A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm
    • Caceres, J. F., G. R. Screaton, and A. R. Krainer. 1998. A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm. Genes Dev. 12:55-66.
    • (1998) Genes Dev. , vol.12 , pp. 55-66
    • Caceres, J.F.1    Screaton, G.R.2    Krainer, A.R.3
  • 3
    • 0031468240 scopus 로고    scopus 로고
    • Both phosphorylation and dephosphorylation of ASF/SF2 are required for pre-mRNA splicing in vitro
    • Cao, W., S. F. Jamison, and M. A. Garcia-Blanco. 1997. Both phosphorylation and dephosphorylation of ASF/SF2 are required for pre-mRNA splicing in vitro. RNA 3:1456-1467.
    • (1997) RNA , vol.3 , pp. 1456-1467
    • Cao, W.1    Jamison, S.F.2    Garcia-Blanco, M.A.3
  • 4
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang, L., and M. Karin. 2001. Mammalian MAP kinase signalling cascades. Nature 410:37-40.
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 5
    • 0030028882 scopus 로고    scopus 로고
    • The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution
    • Colwill, K., T. Pawson, B. Andrews, J. Prasad, J. L. Manley, J. C. Bell, and P. I. Duncan. 1996. The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution. EMBO J. 15:265-275.
    • (1996) EMBO J. , vol.15 , pp. 265-275
    • Colwill, K.1    Pawson, T.2    Andrews, B.3    Prasad, J.4    Manley, J.L.5    Bell, J.C.6    Duncan, P.I.7
  • 6
    • 0029744344 scopus 로고    scopus 로고
    • SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors
    • Colwill, K., L. L. Feng, J. M. Yeakley, G. D. Gish, J. F. Caceres, T. Pawson, and X. D. Fu. 1996. SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors. J. Biol. Chem. 271:24569-24575.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24569-24575
    • Colwill, K.1    Feng, L.L.2    Yeakley, J.M.3    Gish, G.D.4    Caceres, J.F.5    Pawson, T.6    Fu, X.D.7
  • 7
    • 0032923028 scopus 로고    scopus 로고
    • Different tyrosine autophosphorylation requirements in fibroblast growth factor receptor-1 mediate urokinase-type plasminogen activator induction and mitogenesis
    • Dell'Era, P., M. Mohammadi, and M. Presta. 1999. Different tyrosine autophosphorylation requirements in fibroblast growth factor receptor-1 mediate urokinase-type plasminogen activator induction and mitogenesis. Mol. Biol. Cell 10:23-33.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 23-33
    • Dell'Era, P.1    Mohammadi, M.2    Presta, M.3
  • 8
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., R. M. Lebovitz, and R. G. Roeder. 1983. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 9
    • 0032477749 scopus 로고    scopus 로고
    • Spontaneous autophosphorylation of Lyn tyrosine kinase at both its activation segment and C-terminal tail confers altered substrate specificity
    • Donella-Deana, A., L. Cesaro, M. Ruzzene, A. M. Brunati, O. Marin, and L. A. Pinna. 1998. Spontaneous autophosphorylation of Lyn tyrosine kinase at both its activation segment and C-terminal tail confers altered substrate specificity. Biochemistry 37:1438-1446.
    • (1998) Biochemistry , vol.37 , pp. 1438-1446
    • Donella-Deana, A.1    Cesaro, L.2    Ruzzene, M.3    Brunati, A.M.4    Marin, O.5    Pinna, L.A.6
  • 10
    • 0032238550 scopus 로고    scopus 로고
    • Protein phosphorylation plays an essential role in the regulation of alternative splicing and sex determination in Drosophila
    • Du, C., M. E. McGuffin, B. Dauwalder, L. Rabinow, and W. Mattox. 1998. Protein phosphorylation plays an essential role in the regulation of alternative splicing and sex determination in Drosophila. Mol. Cell 2:741-750.
    • (1998) Mol. Cell , vol.2 , pp. 741-750
    • Du, C.1    McGuffin, M.E.2    Dauwalder, B.3    Rabinow, L.4    Mattox, W.5
  • 12
    • 0030863326 scopus 로고    scopus 로고
    • In vivo regulation of alternative pre-mRNA splicing by the Clk1 protein kinase
    • Duncan, P. I., D. F. Stojdl, R. M. Marius, and J. C. Bell. 1997. In vivo regulation of alternative pre-mRNA splicing by the Clk1 protein kinase. Mol. Cell. Biol. 17:5996-6001.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5996-6001
    • Duncan, P.I.1    Stojdl, D.F.2    Marius, R.M.3    Bell, J.C.4
  • 13
    • 0032526770 scopus 로고    scopus 로고
    • The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing
    • Duncan, P. I., D. F. Stojdl, R. M. Marius, K. H. Scheit, and J. C. Bell. 1998. The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing. Exp. Cell. Res. 241:300-308.
    • (1998) Exp. Cell. Res. , vol.241 , pp. 300-308
    • Duncan, P.I.1    Stojdl, D.F.2    Marius, R.M.3    Scheit, K.H.4    Bell, J.C.5
  • 14
    • 0029372979 scopus 로고
    • The superfamily of arginine/serine-rich splicing factors
    • Fu, X. D. 1995. The superfamily of arginine/serine-rich splicing factors. RNA 1:663-680.
    • (1995) RNA , vol.1 , pp. 663-680
    • Fu, X.D.1
  • 15
    • 0037083375 scopus 로고    scopus 로고
    • MAPKK-independent activation of p38α mediated by TAB1-dependent autophosphorylation of p38α
    • Ge, B., H. Gram, F. Di Padova, B. Huang, L. New, R. J. Ulevitch, Y. Luo, and J. Han. 2002. MAPKK-independent activation of p38α mediated by TAB1-dependent autophosphorylation of p38α. Science 295:1291-1294.
    • (2002) Science , vol.295 , pp. 1291-1294
    • Ge, B.1    Gram, H.2    Di Padova, F.3    Huang, B.4    New, L.5    Ulevitch, R.J.6    Luo, Y.7    Han, J.8
  • 16
    • 0025827463 scopus 로고
    • Primary structure of the human splicing factor ASF reveals similarities with Drosophila regulators
    • Ge, H., P. Zuo, and J. L. Manley. 1991. Primary structure of the human splicing factor ASF reveals similarities with Drosophila regulators. Cell 66:373-382.
    • (1991) Cell , vol.66 , pp. 373-382
    • Ge, H.1    Zuo, P.2    Manley, J.L.3
  • 17
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley, B. R. 2000. Sorting out the complexity of SR protein functions. RNA 6:1197-1211.
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 18
    • 0028286596 scopus 로고
    • A serine kinase regulates intracellular localization of splicing factors in the cell cycle
    • Gui, J. F., W. S. Lane, and X. D. Fu. 1994. A serine kinase regulates intracellular localization of splicing factors in the cell cycle. Nature 369:678-682.
    • (1994) Nature , vol.369 , pp. 678-682
    • Gui, J.F.1    Lane, W.S.2    Fu, X.D.3
  • 19
    • 0344074646 scopus 로고    scopus 로고
    • Regulated tissue-specific expression of antagonistic pre-mRNA splicing factors
    • Hanamura, A., J. F. Caceres, A. Mayeda, B. R. Franza, Jr., and A. R. Krainer. 1998. Regulated tissue-specific expression of antagonistic pre-mRNA splicing factors. RNA 4:430-444.
    • (1998) RNA , vol.4 , pp. 430-444
    • Hanamura, A.1    Caceres, J.F.2    Mayeda, A.3    Franza B.R., Jr.4    Krainer, A.R.5
  • 20
    • 0027938872 scopus 로고
    • Characterization by cDNA cloning of two new human protein kinases. Evidence by sequence comparison of a new family of mammalian protein kinases
    • Hanes, J., H. von der Kammer, J. Klaudiny, and K. H. Scheit. 1994. Characterization by cDNA cloning of two new human protein kinases. Evidence by sequence comparison of a new family of mammalian protein kinases. J. Mol. Biol. 244:665-672.
    • (1994) J. Mol. Biol. , vol.244 , pp. 665-672
    • Hanes, J.1    Von der Kammer, H.2    Klaudiny, J.3    Scheit, K.H.4
  • 21
    • 0003448569 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Harlow, E., and D. Lane. 1998. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1998) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 23
    • 0035997377 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II: The role of structure and autoregulation in cellular function
    • 2+/calmodulin-dependent protein kinase II: the role of structure and autoregulation in cellular function. Annu. Rev. Biochem. 71:473-510.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 473-510
    • Hudmon, A.1    Schulman, H.2
  • 24
    • 0032577051 scopus 로고    scopus 로고
    • The phosphorylation of proteins on tyrosine: Its role in cell growth and disease
    • Hunter, T. 1998. The phosphorylation of proteins on tyrosine: its role in cell growth and disease. Philos. Trans. R. Soc. Lond. B Biol. Sci. 353:583-605.
    • (1998) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.353 , pp. 583-605
    • Hunter, T.1
  • 25
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse, M., and J. Kuriyan. 2002. The conformational plasticity of protein kinases. Cell 109:275-282.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 26
    • 0037113942 scopus 로고    scopus 로고
    • Novel SR-related protein Clasp specifically interacts with inactivated Clk4 and induces the exon EB inclusion of Clk
    • Katsu, R., H. Onogi, K. Wada, Y. Kawaguchi, and M. Hagiwara. 2002. Novel SR-related protein Clasp specifically interacts with inactivated Clk4 and induces the exon EB inclusion of Clk. J. Biol. Chem. 277:44220-44228.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44220-44228
    • Katsu, R.1    Onogi, H.2    Wada, K.3    Kawaguchi, Y.4    Hagiwara, M.5
  • 27
  • 28
    • 0033574564 scopus 로고    scopus 로고
    • The subcellular localization of SF2/ASF is regulated by direct interaction with SR protein kinases (SRPKs)
    • Koizumi, J., Y. Okamoto, H. Onogi, A. Mayeda, A. R. Krainer, and M. Hagiwara. 1999. The subcellular localization of SF2/ASF is regulated by direct interaction with SR protein kinases (SRPKs). J. Biol. Chem. 274:11125-11131.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11125-11131
    • Koizumi, J.1    Okamoto, Y.2    Onogi, H.3    Mayeda, A.4    Krainer, A.R.5    Hagiwara, M.6
  • 29
    • 0035943711 scopus 로고    scopus 로고
    • Cloning of human PRP4 reveals interaction with Clk1
    • Kojima, T., T. Zama, K. Wada, H. Onogi, and M. Hagiwara. 2001. Cloning of human PRP4 reveals interaction with Clk1. J. Biol. Chem. 276:32247-32256.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32247-32256
    • Kojima, T.1    Zama, T.2    Wada, K.3    Onogi, H.4    Hagiwara, M.5
  • 30
    • 0035964258 scopus 로고    scopus 로고
    • Transportin-SR2 mediates nuclear import of phosphorylated SR proteins
    • Lai, M. C., R. I. Lin, and W. Y. Tarn. 2001. Transportin-SR2 mediates nuclear import of phosphorylated SR proteins. Proc. Natl. Acad. Sci. USA 98:10154-10159.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10154-10159
    • Lai, M.C.1    Lin, R.I.2    Tarn, W.Y.3
  • 31
    • 0034677884 scopus 로고    scopus 로고
    • A human importin-beta family protein, transportin-SR2, interacts with the phosphorylated RS domain of SR proteins
    • Lai, M. C., R. I. Lin, S. Y. Huang, C. W. Tsai, and W. Y. Tarn. 2000. A human importin-beta family protein, transportin-SR2, interacts with the phosphorylated RS domain of SR proteins. J. Biol. Chem. 275:7950-7957.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7950-7957
    • Lai, M.C.1    Lin, R.I.2    Huang, S.Y.3    Tsai, C.W.4    Tarn, W.Y.5
  • 32
    • 0029910142 scopus 로고    scopus 로고
    • Activity and autophosphorylation of LAMMER protein kinases
    • Lee, K., C. Du, M. Horn, and L. Rabinow. 1996. Activity and autophosphorylation of LAMMER protein kinases. J. Biol. Chem. 271:27299-27303.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27299-27303
    • Lee, K.1    Du, C.2    Horn, M.3    Rabinow, L.4
  • 33
    • 0037117543 scopus 로고    scopus 로고
    • IRAK-4: A noel member of the IRAK family with the properties of an IRAK-kinase
    • Li, S., A. Strelow, E. J. Fontana, and H. Wesche. 2002. IRAK-4: a noel member of the IRAK family with the properties of an IRAK-kinase. Proc. Natl. Acad. Sci. USA 99:5567-5572.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5567-5572
    • Li, S.1    Strelow, A.2    Fontana, E.J.3    Wesche, H.4
  • 34
    • 0029767662 scopus 로고    scopus 로고
    • SR proteins and splicing control
    • Manley, J. L., and R. Tacke. 1996. SR proteins and splicing control. Genes Dev. 10:1569-1579.
    • (1996) Genes Dev. , vol.10 , pp. 1569-1579
    • Manley, J.L.1    Tacke, R.2
  • 35
    • 0033785992 scopus 로고    scopus 로고
    • Biochemical characterization and localization of the dual specificity kinase CLK1
    • Menegay, H. J., M. P. Myers, F. M. Moeslein, and G. E. Landreth. 2000. Biochemical characterization and localization of the dual specificity kinase CLK1. J. Cell Sci. 113:3241-3253.
    • (2000) J. Cell Sci. , vol.113 , pp. 3241-3253
    • Menegay, H.J.1    Myers, M.P.2    Moeslein, F.M.3    Landreth, G.E.4
  • 36
    • 0028043718 scopus 로고
    • Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism
    • Mermoud, J. E., P. T. Cohen, and A. I. Lamond. 1994. Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism. EMBO J. 13:5679-5688.
    • (1994) EMBO J. , vol.13 , pp. 5679-5688
    • Mermoud, J.E.1    Cohen, P.T.2    Lamond, A.I.3
  • 37
    • 0033602473 scopus 로고    scopus 로고
    • RNA splicing: What has phosphorylation got to do with it?
    • Misteli, T. 1999. RNA splicing: what has phosphorylation got to do with it? Curt. Biol. 9:R198-R200.
    • (1999) Curt. Biol. , vol.9
    • Misteli, T.1
  • 38
    • 1842376906 scopus 로고    scopus 로고
    • The dynamics of a pre-mRNA splicing factor in living cells
    • Misteli, T., J. F. Caceres, and D. L. Spector. 1997. The dynamics of a pre-mRNA splicing factor in living cells. Nature 387:523-527.
    • (1997) Nature , vol.387 , pp. 523-527
    • Misteli, T.1    Caceres, J.F.2    Spector, D.L.3
  • 39
    • 0032547829 scopus 로고    scopus 로고
    • Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo
    • Misteli, T., J. F. Caceres, J. Q. Clement, A. R. Krainer, M. F. Wilkinson, and D. L. Spector. 1998. Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo. J. Cell Biol. 143:297-307.
    • (1998) J. Cell Biol. , vol.143 , pp. 297-307
    • Misteli, T.1    Caceres, J.F.2    Clement, J.Q.3    Krainer, A.R.4    Wilkinson, M.F.5    Spector, D.L.6
  • 40
    • 0035393343 scopus 로고    scopus 로고
    • Genome-wide detection of alternative splicing in expressed sequences of human genes
    • Modrek, B., A. Resch, C. Grasso, and C. Lee. 2001. Genome-wide detection of alternative splicing in expressed sequences of human genes. Nucleic Acids Res. 29:2850-2859.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2850-2859
    • Modrek, B.1    Resch, A.2    Grasso, C.3    Lee, C.4
  • 41
    • 0033578839 scopus 로고    scopus 로고
    • The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B
    • Moeslein, F. M., M. P. Myers, and G. E. Landreth. 1999. The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B. J. Biol. Chem. 274:26697-26704.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26697-26704
    • Moeslein, F.M.1    Myers, M.P.2    Landreth, G.E.3
  • 42
    • 0032901297 scopus 로고    scopus 로고
    • The type 2C Ser/Thr phosphatase PP2Cγ is a pre-mRNA splicing factor
    • Murray, M. V., R. Kobayashi, and A. R. Krainer. 1999. The type 2C Ser/Thr phosphatase PP2Cγ is a pre-mRNA splicing factor. Genes Dev. 13:87-97.
    • (1999) Genes Dev. , vol.13 , pp. 87-97
    • Murray, M.V.1    Kobayashi, R.2    Krainer, A.R.3
  • 43
    • 0030778935 scopus 로고    scopus 로고
    • Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
    • Nayler, O., S. Stamm, and A. Ullrich. 1997. Characterization and comparison of four serine- and arginine-rich (SR) protein kinases. Biochem. J. 326:693-700.
    • (1997) Biochem. J. , vol.326 , pp. 693-700
    • Nayler, O.1    Stamm, S.2    Ullrich, A.3
  • 44
    • 0032545381 scopus 로고    scopus 로고
    • The cellular localization of the murine serine/arginine-rich protein kinase CLK2 is regulated by serine 141 autophosphorylation
    • Nayler, O., F. Schnorrer, S. Stamm, and A. Ullrich. 1998. The cellular localization of the murine serine/arginine-rich protein kinase CLK2 is regulated by serine 141 autophosphorylation. J. Biol. Chem. 273:34341-34348.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34341-34348
    • Nayler, O.1    Schnorrer, F.2    Stamm, S.3    Ullrich, A.4
  • 45
    • 0029050868 scopus 로고
    • A conserved epitope on a subset of SR proteins defines a larger family of pre-mRNA splicing factors
    • Neugebauer, K. M., J. A. Stolk, and M. B. Roth. 1995. A conserved epitope on a subset of SR proteins defines a larger family of pre-mRNA splicing factors. J. Cell Biol. 129:899-908.
    • (1995) J. Cell Biol. , vol.129 , pp. 899-908
    • Neugebauer, K.M.1    Stolk, J.A.2    Roth, M.B.3
  • 46
    • 0037065728 scopus 로고    scopus 로고
    • Phosphorylation by LAMMER protein kinases: Determination of a consensus site, identification of in vitro substrates, and implications for substrate preferences
    • Nikolakaki, E., C. Du, J. Lai, T. Giannakouros, L. Cantley, and L. Rabinow. 2002. Phosphorylation by LAMMER protein kinases: determination of a consensus site, identification of in vitro substrates, and implications for substrate preferences. Biochemistry 41:2055-2066.
    • (2002) Biochemistry , vol.41 , pp. 2055-2066
    • Nikolakaki, E.1    Du, C.2    Lai, J.3    Giannakouros, T.4    Cantley, L.5    Rabinow, L.6
  • 47
    • 0032827418 scopus 로고    scopus 로고
    • The protein kinase Clk/Sty directly modulates SR protein activity: Both hyper- and hypophosphorylation inhibit splicing
    • Prasad, J., K. Colwill, T. Pawson, and J. L. Manley. 1999. The protein kinase Clk/Sty directly modulates SR protein activity: both hyper- and hypophosphorylation inhibit splicing. Mol. Cell. Biol. 19:6991-7000.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6991-7000
    • Prasad, J.1    Colwill, K.2    Pawson, T.3    Manley, J.L.4
  • 48
    • 0037017406 scopus 로고    scopus 로고
    • Disassembly of interchromatin granule clusters alters the coordination of transcription and pre-mRNA splicing
    • Sacco-Bubulya, P., and D. L. Spector. 2002. Disassembly of interchromatin granule clusters alters the coordination of transcription and pre-mRNA splicing. J. Cell Biol. 156:425-436.
    • (2002) J. Cell Biol. , vol.156 , pp. 425-436
    • Sacco-Bubulya, P.1    Spector, D.L.2
  • 49
    • 0035964316 scopus 로고    scopus 로고
    • Regulation of SR protein localization during development
    • Sanford, J. R., and J. P. Bruzik. 2001. Regulation of SR protein localization during development. Proc. Natl. Acad. Sci. USA 98:10184-10189.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10184-10189
    • Sanford, J.R.1    Bruzik, J.P.2
  • 50
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. 2000. Cell signaling by receptor tyrosine kinases. Cell 103:211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 51
    • 0036336519 scopus 로고    scopus 로고
    • Pelle kinase is activated by autophosphorylation during Toll signaling in Drosophila
    • Shen, B., and J. L. Manley. 2002. Pelle kinase is activated by autophosphorylation during Toll signaling in Drosophila. Development 129:1925-1933.
    • (2002) Development , vol.129 , pp. 1925-1933
    • Shen, B.1    Manley, J.L.2
  • 52
    • 0032737702 scopus 로고    scopus 로고
    • SR protein kinases: The splice of life
    • Stojdl, D. F., and J. C. Bell. 1999. SR protein kinases: the splice of life. Biochem. Cell Biol. 77:293-298.
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 293-298
    • Stojdl, D.F.1    Bell, J.C.2
  • 53
    • 0031037690 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by an SR protein requires RS domain phosphorylation: Creation of an SRp40-specific splicing enhancer
    • Tacke, R., Y. Chen, and J. L. Manley. 1997. Sequence-specific RNA binding by an SR protein requires RS domain phosphorylation: creation of an SRp40-specific splicing enhancer. Proc. Natl. Acad. Sci. USA 94:1148-1153.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1148-1153
    • Tacke, R.1    Chen, Y.2    Manley, J.L.3
  • 54
    • 0032478506 scopus 로고    scopus 로고
    • Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing
    • Tacke, R., M. Tohyama, S. Ogawa, and J. L. Manley. 1998. Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing. Cell 93:139-148.
    • (1998) Cell , vol.93 , pp. 139-148
    • Tacke, R.1    Tohyama, M.2    Ogawa, S.3    Manley, J.L.4
  • 55
    • 0033152209 scopus 로고    scopus 로고
    • Determinants of SR protein specificity
    • Tacke, R., and J. L. Manley. 1999. Determinants of SR protein specificity. Curr. Opin. Cell Biol. 11:358-362.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 358-362
    • Tacke, R.1    Manley, J.L.2
  • 57
    • 0007570010 scopus 로고    scopus 로고
    • The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation
    • van der Houven van Oordt, W., M. T. Diaz-Meco, J. Lozano, A. R. Krainer, J. Moscat, and J. F. Caceres. 2000. The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation. J. Cell Biol. 149:307-316.
    • (2000) J. Cell Biol. , vol.149 , pp. 307-316
    • Van der Houven van Oordt, W.1    Diaz-Meco, M.T.2    Lozano, J.3    Krainer, A.R.4    Moscat, J.5    Caceres, J.F.6
  • 58
    • 0032559642 scopus 로고    scopus 로고
    • SRPK2: A differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells
    • Wang, H. Y., W. Lin, J. A. Dyck, J. M. Yeakley, Z. Songyang, L. C. Cantley, and X. D. Fu. 1998. SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells. J. Cell Biol. 140:737-750.
    • (1998) J. Cell Biol. , vol.140 , pp. 737-750
    • Wang, H.Y.1    Lin, W.2    Dyck, J.A.3    Yeakley, J.M.4    Songyang, Z.5    Cantley, L.C.6    Fu, X.D.7
  • 59
    • 0029295349 scopus 로고
    • Overexpression of the SR proteins ASF/SF2 and SC35 influences alternative splicing in vivo in diverse ways
    • Wang, J., and J. L. Manley. 1995. Overexpression of the SR proteins ASF/SF2 and SC35 influences alternative splicing in vivo in diverse ways. RNA 1:335-346.
    • (1995) RNA , vol.1 , pp. 335-346
    • Wang, J.1    Manley, J.L.2
  • 60
    • 0028176021 scopus 로고
    • Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation
    • Wang, Q. M., C. J. Fiol, A. A. DePaoli-Roach, and P. J. Roach. 1994. Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation. J. Biol. Chem. 269:14566-14574.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14566-14574
    • Wang, Q.M.1    Fiol, C.J.2    DePaoli-Roach, A.A.3    Roach, P.J.4
  • 61
    • 0027137934 scopus 로고
    • Specific interactions between proteins implicated in splice site selection and regulated alternative splicing
    • Wu, J. Y., and T. Maniatis. 1993. Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell 75:1061-1070.
    • (1993) Cell , vol.75 , pp. 1061-1070
    • Wu, J.Y.1    Maniatis, T.2
  • 62
    • 0031042396 scopus 로고    scopus 로고
    • Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing
    • Xiao, S. H., and J. L. Manley. 1997. Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing. Genes Dev. 11:334-344.
    • (1997) Genes Dev. , vol.11 , pp. 334-344
    • Xiao, S.H.1    Manley, J.L.2
  • 63
    • 0032476604 scopus 로고    scopus 로고
    • Phosphorylation-dephosphorylation differentially affects activities of splicing factor ASF/SF2
    • Xiao, S. H., and J. L. Manley. 1998. Phosphorylation-dephosphorylation differentially affects activities of splicing factor ASF/SF2. EMBO J. 17:6359-6367.
    • (1998) EMBO J. , vol.17 , pp. 6359-6367
    • Xiao, S.H.1    Manley, J.L.2
  • 64
    • 0033786972 scopus 로고    scopus 로고
    • The LAMMER protein kinase encoded by the Doa locus of Drosophila is required in both somatic and germline cells and is expressed as both nuclear and cytoplasmic isoforms throughout development
    • Yun, B., K. Lee, R. Farka, C. Hitte, and L. Rabinow. 2000. The LAMMER protein kinase encoded by the Doa locus of Drosophila is required in both somatic and germline cells and is expressed as both nuclear and cytoplasmic isoforms throughout development. Genetics 156:749-761.
    • (2000) Genetics , vol.156 , pp. 749-761
    • Yun, B.1    Lee, K.2    Farka, R.3    Hitte, C.4    Rabinow, L.5
  • 65
    • 0027160003 scopus 로고
    • Distinct functions of SR proteins in alternative pre-mRNA splicing
    • Zahler, A. M., K. M. Neugebauer, W. S. Lane, and M. B. Roth. 1993. Distinct functions of SR proteins in alternative pre-mRNA splicing. Science 260:219-222.
    • (1993) Science , vol.260 , pp. 219-222
    • Zahler, A.M.1    Neugebauer, K.M.2    Lane, W.S.3    Roth, M.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.