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Volumn 267, Issue 14, 2000, Pages 4456-4464

Specific Ser-Pro, phosphorylation by the RNA-recognition motif containing kinase KIS

Author keywords

Consensus sequence motif; KIS; Phosphorylation site; Protein kinase; RNA recognition motif

Indexed keywords

KINASE INTERACTING WITH STATHMIN; MYELIN BASIC PROTEIN; RNA BINDING PROTEIN; SYNAPSIN I; UNCLASSIFIED DRUG;

EID: 0033942006     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01493.x     Document Type: Article
Times cited : (22)

References (36)
  • 1
    • 0030028882 scopus 로고    scopus 로고
    • The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution
    • 1. Colwill, K., Pawson, T., Andrews, B., Prasad, J., Manley, J.L., Bell, J.C. & Duncan, P.I. (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
  • 2
    • 0033575670 scopus 로고    scopus 로고
    • Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly
    • 2. Wang, X., Bruderer, S., Rafi, Z., Xue, J., Milburn, P.J., Krämer, A. & Robinson, P.J. (1996) Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly. EMBO J. 18, 4549-4559.
    • (1996) EMBO J. , vol.18 , pp. 4549-4559
    • Wang, X.1    Bruderer, S.2    Rafi, Z.3    Xue, J.4    Milburn, P.J.5    Krämer, A.6    Robinson, P.J.7
  • 3
    • 0033574564 scopus 로고    scopus 로고
    • The subcellular localization of SF2/ASF is regulated by direct interaction with SR protein kinases (SRPKs)
    • 3. Koisumi, J., Okamoto, Y., Onogi, H., Mayeda, A., Krainer, A.R. & Hagiwara, M. (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
    • Koisumi, J.1    Okamoto, Y.2    Onogi, H.3    Mayeda, A.4    Krainer, A.R.5    Hagiwara, M.6
  • 4
    • 0344654761 scopus 로고    scopus 로고
    • Phosphorylation regulates in vivo interaction and molecular targeting of serine/arginine-rich pre-mRNA splicing factors
    • 4. Yeakley, J.M., Tronchère, H., Olesen, J., Dyck, J.A., Wang, H.-Y. & Fu, X.-D. (1999) Phosphorylation regulates in vivo interaction and molecular targeting of serine/arginine-rich pre-mRNA splicing factors. J. Cell Biol. 145, 447-455.
    • (1999) J. Cell Biol. , vol.145 , pp. 447-455
    • Yeakley, J.M.1    Tronchère, H.2    Olesen, J.3    Dyck, J.A.4    Wang, H.-Y.5    Fu, X.-D.6
  • 5
    • 0032737702 scopus 로고    scopus 로고
    • SR protein kinases: The splice of life
    • 5. Stojdl, D.F. & Bell, J.C. (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
  • 6
    • 0033213918 scopus 로고    scopus 로고
    • Translation initiation: Adept at adapting
    • 6. Dever, T.E. (1999) Translation initiation: adept at adapting. Trends Biochem. Sci. 24, 398-403.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 398-403
    • Dever, T.E.1
  • 7
    • 0028943627 scopus 로고
    • Stathmin interaction with a novel putative kinase and coiled-coil forming protein domains
    • 7. Maucuer, A., Camonis, J.H. & Sobel, A. (1995) Stathmin interaction with a novel putative kinase and coiled-coil forming protein domains. Proc. Natl Acad. Sci. USA 92, 3100-3104.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3100-3104
    • Maucuer, A.1    Camonis, J.H.2    Sobel, A.3
  • 9
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors
    • 9. Birney, E., Kumar, S. & Krainer, A.R. (1993) Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res. 21, 5803-5816.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3
  • 10
    • 0025745372 scopus 로고
    • Stathmin: A relay phosphoprotein for multiple signal transduction?
    • 10. Sobel, A. (1991) Stathmin: a relay phosphoprotein for multiple signal transduction? Trends Biochem. Sci. 16, 301-305.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 301-305
    • Sobel, A.1
  • 12
    • 0024509921 scopus 로고
    • Intracellular substrates for extracellular signaling: Characterization of a ubiquitous, neuron-enriched phosphoprotein (Stathmin)
    • 12. Sobel, A., Boutterin, M.C., Beretta, L., Chneiweiss, H., Doye, V. & Peyro-Saint-Paul, H. (1989) Intracellular substrates for extracellular signaling: characterization of a ubiquitous, neuron-enriched phosphoprotein (Stathmin). J. Biol. Chem. 264, 3765-3772.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3765-3772
    • Sobel, A.1    Boutterin, M.C.2    Beretta, L.3    Chneiweiss, H.4    Doye, V.5    Peyro-Saint-Paul, H.6
  • 13
    • 0030750560 scopus 로고    scopus 로고
    • Control of microtubule dynamics by oncoprotein 18: Dissection of the regulatory role of multisite phosphorylation during mitosis
    • 13. Larsson, N., Marklund, U., Gradin, H.M., Brattsand, G. & Gullberg, M. (1997) Control of microtubule dynamics by oncoprotein 18: dissection of the regulatory role of multisite phosphorylation during mitosis. Mol. Cell. Biol. 17, 5530-5539.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5530-5539
    • Larsson, N.1    Marklund, U.2    Gradin, H.M.3    Brattsand, G.4    Gullberg, M.5
  • 14
    • 0030968633 scopus 로고    scopus 로고
    • The microtubule-destabilizing activity of metablastin (p19) is controlled by phosphorylation
    • 14. Horwitz, S.B., Shen, H.-J., He, L., Dittmar, P., Neef, R., Chen, J. & Schubart, U.K. (1997) The microtubule-destabilizing activity of metablastin (p19) is controlled by phosphorylation. J. Biol. Chem. 272, 8129-8132.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8129-8132
    • Horwitz, S.B.1    Shen, H.-J.2    He, L.3    Dittmar, P.4    Neef, R.5    Chen, J.6    Schubart, U.K.7
  • 15
    • 0030048731 scopus 로고    scopus 로고
    • Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
    • 15. Belmont, L.D. & Mitchison, T.J. (1996) Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules. Cell 84, 623-631.
    • (1996) Cell , vol.84 , pp. 623-631
    • Belmont, L.D.1    Mitchison, T.J.2
  • 16
    • 0031745447 scopus 로고    scopus 로고
    • The stathmin phosphoprotein family: Intracellular localization and effects on the microtubule network
    • 16. Gavet, O., Ozon, S., Manceau, V., Lawler, S., Curmi, P. & Sobel, A. (1998) The stathmin phosphoprotein family: intracellular localization and effects on the microtubule network. J. Cell Sci. 111, 3333-3346.
    • (1998) J. Cell Sci. , vol.111 , pp. 3333-3346
    • Gavet, O.1    Ozon, S.2    Manceau, V.3    Lawler, S.4    Curmi, P.5    Sobel, A.6
  • 18
    • 10344242949 scopus 로고    scopus 로고
    • Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme
    • 18. Rashidul Alam, M., Caldwell, B.D., Johnson, R.C., Darlington, D.N., Mains, R.E. & Eipper, B.A. (1996) Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme. J. Biol. Chem. 271, 28636-28640.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28636-28640
    • Rashidul Alam, M.1    Caldwell, B.D.2    Johnson, R.C.3    Darlington, D.N.4    Mains, R.E.5    Eipper, B.A.6
  • 19
    • 0030595187 scopus 로고    scopus 로고
    • Interaction of U2af65 RS region with pre-mRNA of branch point and promotion base pairing with U2 snRNA
    • 19. Valcàrcel, J., Gaur, R.K., Singh, R. & Green, M.R. (1996) Interaction of U2af65 RS region with pre-mRNA of branch point and promotion base pairing with U2 snRNA. Science 273, 1709.
    • (1996) Science , vol.273 , pp. 1709
    • Valcàrcel, J.1    Gaur, R.K.2    Singh, R.3    Green, M.R.4
  • 20
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • 20. Pearson, R.B. & Kemp, B.E. (1991) Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. Methods Enzymol. 200, 62-81.
    • (1991) Methods Enzymol. , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 21
    • 0030581751 scopus 로고    scopus 로고
    • How do protein kinases recognize their substrates?
    • 21. Pinna, L.A. & Ruzzene, M. (1996) How do protein kinases recognize their substrates? Biochem. Biophys. Acta 1314, 191-225.
    • (1996) Biochem. Biophys. Acta , vol.1314 , pp. 191-225
    • Pinna, L.A.1    Ruzzene, M.2
  • 22
    • 0028362176 scopus 로고
    • Molecular characterization of human stathmin expressed in Escherichia coli: Site-directed mutagenesis of two phosphorylatable serines (Ser-25 and Ser-63)
    • 22. Curmi, P., Maucuer, A., Asselin, S., Lecourtois, M., Chaffotte, A., Schmitter, J.M. & Sobel, A. (1994) Molecular characterization of human stathmin expressed in Escherichia coli: site-directed mutagenesis of two phosphorylatable serines (Ser-25 and Ser-63). Biochem. J. 300, 331-338.
    • (1994) Biochem. J. , vol.300 , pp. 331-338
    • Curmi, P.1    Maucuer, A.2    Asselin, S.3    Lecourtois, M.4    Chaffotte, A.5    Schmitter, J.M.6    Sobel, A.7
  • 23
    • 0030470273 scopus 로고    scopus 로고
    • Phosphorylation site specificity of the cdc2-related kinase PITALRE
    • 23. Garriga, J., Segura, E., Mayol, X., Grubmeyer, C. & Graña, X. (1996) Phosphorylation site specificity of the cdc2-related kinase PITALRE. Biochem. J. 320, 983-989.
    • (1996) Biochem. J. , vol.320 , pp. 983-989
    • Garriga, J.1    Segura, E.2    Mayol, X.3    Grubmeyer, C.4    Graña, X.5
  • 24
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • 24. Boyle, W.J., van der Geer, P. & Hunter, T. (1991) Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol 201, 110-149.
    • (1991) Methods Enzymol , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 25
    • 0032560583 scopus 로고    scopus 로고
    • Statistical analysis of protein kinase specificity determinants
    • 25. Kreegipuu, A., Blom, N., Brunak, S. & Järv, J. (1998) Statistical analysis of protein kinase specificity determinants. FEBS Lett. 430, 45-50.
    • (1998) FEBS Lett. , vol.430 , pp. 45-50
    • Kreegipuu, A.1    Blom, N.2    Brunak, S.3    Järv, J.4
  • 28
    • 0028773477 scopus 로고
    • Three protein kinase structures define a common motif
    • 28. Taylor, S.S. & Radzio-Andzelm, E. (1994) Three protein kinase structures define a common motif. Structure 2, 345-355.
    • (1994) Structure , vol.2 , pp. 345-355
    • Taylor, S.S.1    Radzio-Andzelm, E.2
  • 29
    • 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
    • 29. Wang, H.-Y., Lin, W., Dyck, J.A., Yeakley, J.M., Songiang, Z., Cantley, L.C. & Fu, X.-D. (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    Songiang, Z.5    Cantley, L.C.6    Fu, X.-D.7
  • 30
    • 0028176874 scopus 로고
    • 97-Pro in brain myelin basic protein: Evidence for Thr-Pro and Ser-Arg-X-X-Ser as consensus sequence motifs
    • 97-Pro in brain myelin basic protein: evidence for Thr-Pro and Ser-Arg-X-X-Ser as consensus sequence motifs. J. Neurochem. 62, 1596-1603.
    • (1994) J. Neurochem. , vol.62 , pp. 1596-1603
    • Yu, J.-S.1    Yang, S.-D.2
  • 32
    • 0025018057 scopus 로고
    • Identification of the sites in myelin basic protein that are phosphorylated by meiosis-activated protein kinase p44mpk
    • 32. Sanghera, J.S., Aebersold, R., Morrison, H.D., Bures, E.J. & Pelech, S.L. (1990) Identification of the sites in myelin basic protein that are phosphorylated by meiosis-activated protein kinase p44mpk. FEBS Lett. 273, 223-226.
    • (1990) FEBS Lett. , vol.273 , pp. 223-226
    • Sanghera, J.S.1    Aebersold, R.2    Morrison, H.D.3    Bures, E.J.4    Pelech, S.L.5
  • 33
    • 0025258896 scopus 로고
    • Identification by mass spectrometry of threonine 97 in bovine myelin basic protein as a specific phosphorylation site for mitogen-activated protein kinase
    • 33. Erickson, A.K., Payne, D.M., Martino, P.A., Rossomando, A.J., Shabanowitz, J., Weber, M.J., Hunt, D.F. & Sturgill, T.W. (1990) Identification by mass spectrometry of threonine 97 in bovine myelin basic protein as a specific phosphorylation site for mitogen-activated protein kinase. J. Biol. Chem. 265, 19728-19735.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19728-19735
    • Erickson, A.K.1    Payne, D.M.2    Martino, P.A.3    Rossomando, A.J.4    Shabanowitz, J.5    Weber, M.J.6    Hunt, D.F.7    Sturgill, T.W.8
  • 34
    • 0032562138 scopus 로고    scopus 로고
    • Determination of the sites of posttranscriptional modifications in the charge isomers of bovine myelin basic protein by capillary electrophoresis-mass spectromelry
    • 34. Zand, R., Li, X.L., Jin, X. & Lubman, D.M. (1998) Determination of the sites of posttranscriptional modifications in the charge isomers of bovine myelin basic protein by capillary electrophoresis-mass spectromelry. Biochemistry 37, 2441-2449.
    • (1998) Biochemistry , vol.37 , pp. 2441-2449
    • Zand, R.1    Li, X.L.2    Jin, X.3    Lubman, D.M.4
  • 35
    • 0020673319 scopus 로고
    • Identification of multiple in vivo phosphorylation sites in rabbit myelin basic protein
    • 35. Martenson, R.E., Law, M.J. & Deitch, J.S. (1983) Identification of multiple in vivo phosphorylation sites in rabbit myelin basic protein. J. Biol. Chem. 258, 930-937.
    • (1983) J. Biol. Chem. , vol.258 , pp. 930-937
    • Martenson, R.E.1    Law, M.J.2    Deitch, J.S.3
  • 36
    • 0030946002 scopus 로고    scopus 로고
    • The active transport of myelin basic protein into the nucleus suggests a regulatory role in myelination
    • 36. Pedraza, L., Fidler, L., Staugailis, S.M. & Colman, D.R. (1997) The active transport of myelin basic protein into the nucleus suggests a regulatory role in myelination. Neuron 18, 579-589.
    • (1997) Neuron , vol.18 , pp. 579-589
    • Pedraza, L.1    Fidler, L.2    Staugailis, S.M.3    Colman, D.R.4


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