메뉴 건너뛰기




Volumn 50, Issue 32, 2011, Pages 6888-6900

Applying the brakes to multisite SR protein phosphorylation: Substrate-induced effects on the splicing kinase SRPK1

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING AFFINITIES; ENZYME-SUBSTRATE COMPLEXES; EXCHANGE RATES; KINETIC EXPERIMENT; KINETIC MECHANISM; MULTI-SITE; MUTAGENESIS EXPERIMENT; N-TERMINALS; PHOSPHORYL TRANSFER; PROTEIN KINASE; PROTEIN SUBSTRATE; RAPID QUENCH; REACTION COORDINATES; SITE-SPECIFIC; SPLICING FACTORS; SR PROTEIN;

EID: 80051521166     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2007993     Document Type: Article
Times cited : (16)

References (41)
  • 1
    • 0042671357 scopus 로고    scopus 로고
    • Pre-mRNA splicing: Awash in a sea of proteins
    • DOI 10.1016/S1097-2765(03)00270-3
    • Jurica, M. S. and Moore, M. J. (2003) Pre-mRNA splicing: awash in a sea of proteins Mol. Cell 12, 5-14 (Pubitemid 36945033)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 5-14
    • Jurica, M.S.1    Moore, M.J.2
  • 2
    • 0032710804 scopus 로고    scopus 로고
    • SR-related proteins and the processing of messenger RNA precursors
    • DOI 10.1139/bcb-77-4-277
    • Blencowe, B. J., Bowman, J. A., McCracken, S., and Rosonina, E. (1999) SR-related proteins and the processing of messenger RNA precursors Biochem. Cell Biol. 77, 277-291 (Pubitemid 29531851)
    • (1999) Biochemistry and Cell Biology , vol.77 , Issue.4 , pp. 277-291
    • Blencowe, B.J.1    Bowman, J.A.L.2    McCracken, S.3    Rosonina, E.4
  • 3
    • 0028286596 scopus 로고
    • A serine kinase regulates intracellular localization of splicing factors in the cell cycle
    • DOI 10.1038/369678a0
    • Gui, J. F., Lane, W. S., and Fu, X. D. (1994) A serine kinase regulates intracellular localization of splicing factors in the cell cycle Nature 369, 678-682 (Pubitemid 24199476)
    • (1994) Nature , vol.369 , Issue.6482 , pp. 678-682
    • Gui, J.-F.1    Lane, W.S.2    Fu, X.-D.3
  • 5
    • 61449176062 scopus 로고    scopus 로고
    • Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones
    • Zhong, X. Y., Ding, J. H., Adams, J. A., Ghosh, G., and Fu, X. D. (2009) Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones Genes Dev. 23, 482-495
    • (2009) Genes Dev. , vol.23 , pp. 482-495
    • Zhong, X.Y.1    Ding, J.H.2    Adams, J.A.3    Ghosh, G.4    Fu, X.D.5
  • 6
    • 0027137934 scopus 로고
    • Specific interactions between proteins implicated in splice site selection and regulated alternative splicing
    • DOI 10.1016/0092-8674(93)90316-I
    • Wu, J. Y. and Maniatis, T. (1993) Specific interactions between proteins implicated in splice site selection and regulated alternative splicing Cell 75, 1061-1070 (Pubitemid 24006103)
    • (1993) Cell , vol.75 , Issue.6 , pp. 1061-1070
    • Wu, J.Y.1    Maniatis, T.2
  • 7
    • 0028289188 scopus 로고
    • Protein-protein interactions and 5-2-splice-site recognition in mammalian mRNA precursors
    • Kohtz, J. D., Jamison, S. F., Will, C. L., Zuo, P., Luhrmann, R., Garcia-Blanco, M. A., and Manley, J. L. (1994) Protein-protein interactions and 5-2-splice-site recognition in mammalian mRNA precursors Nature 368, 119-124
    • (1994) Nature , vol.368 , pp. 119-124
    • Kohtz, J.D.1    Jamison, S.F.2    Will, C.L.3    Zuo, P.4    Luhrmann, R.5    Garcia-Blanco, M.A.6    Manley, J.L.7
  • 9
    • 33646792573 scopus 로고    scopus 로고
    • SRp30a (ASF/SF2) regulates the alternative splicing of caspase-9 pre-mRNA and is required for ceramide-responsiveness
    • DOI 10.1194/jlr.C600003-JLR200
    • Massiello, A. and Chalfant, C. E. (2006) SRp30a (ASF/SF2) regulates the alternative splicing of caspase-9 pre-mRNA and is required for ceramide-responsiveness J. Lipid Res. 47, 892-897 (Pubitemid 43764686)
    • (2006) Journal of Lipid Research , vol.47 , Issue.5 , pp. 892-897
    • Massiello, A.1    Chalfant, C.E.2
  • 10
    • 0038401969 scopus 로고    scopus 로고
    • Role of the modular domains of SR proteins in subnuclear localization and alternative splicing specificity
    • DOI 10.1083/jcb.138.2.225
    • Caceres, J. F., Misteli, T., Screaton, G. R., Spector, D. L., and Krainer, A. R. (1997) Role of the modular domains of SR proteins in subnuclear localization and alternative splicing specificity J. Cell Biol. 138, 225-238 (Pubitemid 27323527)
    • (1997) Journal of Cell Biology , vol.138 , Issue.2 , pp. 225-238
    • Caceres, J.F.1    Misteli, T.2    Screaton, G.R.3    Spector, D.L.4    Krainer, A.R.5
  • 11
    • 0033553882 scopus 로고    scopus 로고
    • Transportin-SR, a nuclear import receptor for SR proteins
    • DOI 10.1083/jcb.145.6.1145
    • Kataoka, N., Bachorik, J. L., and Dreyfuss, G. (1999) Transportin-SR, a nuclear import receptor for SR proteins J. Cell Biol. 145, 1145-1152 (Pubitemid 29293627)
    • (1999) Journal of Cell Biology , vol.145 , Issue.6 , pp. 1145-1152
    • Kataoka, N.1    Bachorik, J.L.2    Dreyfuss, G.3
  • 12
    • 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., Lin, R. I., Huang, S. Y., Tsai, C. W., and Tarn, W. Y. (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
  • 14
    • 67649306195 scopus 로고    scopus 로고
    • Regiospecific phosphorylation control of the SR protein ASF/SF2 by SRPK1
    • Ma, C. T., Hagopian, J. C., Ghosh, G., Fu, X. D., and Adams, J. A. (2009) Regiospecific phosphorylation control of the SR protein ASF/SF2 by SRPK1 J. Mol. Biol. 390, 618-634
    • (2009) J. Mol. Biol. , vol.390 , pp. 618-634
    • Ma, C.T.1    Hagopian, J.C.2    Ghosh, G.3    Fu, X.D.4    Adams, J.A.5
  • 18
    • 40649092847 scopus 로고    scopus 로고
    • A Sliding Docking Interaction Is Essential for Sequential and Processive Phosphorylation of an SR Protein by SRPK1
    • DOI 10.1016/j.molcel.2007.12.017, PII S1097276508000129
    • Ngo, J. C., Giang, K., Chakrabarti, S., Ma, C. T., Huynh, N., Hagopian, J. C., Dorrestein, P. C., Fu, X. D., Adams, J. A., and Ghosh, G. (2008) A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1 Mol. Cell 29, 563-576 (Pubitemid 351374682)
    • (2008) Molecular Cell , vol.29 , Issue.5 , pp. 563-576
    • Ngo, J.C.K.1    Giang, K.2    Chakrabarti, S.3    Ma, C.-T.4    Huynh, N.5    Hagopian, J.C.6    Dorrestein, P.C.7    Fu, X.-D.8    Adams, J.A.9    Ghosh, G.10
  • 19
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • DOI 10.1021/cr000230w
    • Adams, J. A. (2001) Kinetic and Catalytic Mechanisms of Protein Kinases Chem. Rev. 101, 2271-2290 (Pubitemid 35373019)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2271-2290
    • Adams, J.A.1
  • 20
    • 0017638132 scopus 로고
    • Role of multiple basic residues in determining the substrate specificity of cyclic AMP dependent protein kinase
    • Kemp, B. E., Graves, D. J., Benjamini, E., and Krebs, E. G. (1977) Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase J. Biol. Chem. 252, 4888-4894 (Pubitemid 8162200)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.14 , pp. 4888-4894
    • Kemp, B.E.1    Graves, D.J.2    Benjamini, E.3    Krebs, E.G.4
  • 21
    • 0026698850 scopus 로고
    • Energetic limits of phosphotransfer in the catalytic subunit of cAMP- dependent protein kinase as measured by viscosity experiments
    • Adams, J. A. and Taylor, S. S. (1992) Energetic limits of phosphotransfer in the catalytic subunit of cAMP- dependent protein kinase as measured by viscosity experiments Biochemistry 31, 8516-8522
    • (1992) Biochemistry , vol.31 , pp. 8516-8522
    • Adams, J.A.1    Taylor, S.S.2
  • 22
    • 0028903531 scopus 로고
    • Transient kinetic approaches to enzyme mechanisms
    • Fierke, C. A. and Hammes, G. G. (1995) Transient kinetic approaches to enzyme mechanisms Methods Enzymol. 249, 3-37
    • (1995) Methods Enzymol. , vol.249 , pp. 3-37
    • Fierke, C.A.1    Hammes, G.G.2
  • 23
    • 0030049479 scopus 로고    scopus 로고
    • Pre-steady-state kinetic analysis of cAMP-dependent protein kinase using rapid quench flow techniques
    • DOI 10.1021/bi952144+
    • Grant, B. D. and Adams, J. A. (1996) Pre-steady-state kinetic analysis of cAMP-dependent protein kinase using rapid quench flow techniques Biochemistry 35, 2022-2029 (Pubitemid 26062652)
    • (1996) Biochemistry , vol.35 , Issue.6 , pp. 2022-2029
    • Grant, B.D.1    Adams, J.A.2
  • 24
    • 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
    • DOI 10.1083/jcb.140.4.737
    • Wang, H. Y., Lin, W., Dyck, J. A., Yeakley, J. M., Songyang, Z., Cantley, L. C., and 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 (Pubitemid 28141214)
    • (1998) Journal of Cell Biology , vol.140 , Issue.4 , 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
  • 25
    • 0020484823 scopus 로고
    • Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variation
    • Brouwer, A. C. and Kirsch, J. F. (1982) Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variation Biochemistry 21, 1302-1307
    • (1982) Biochemistry , vol.21 , pp. 1302-1307
    • Brouwer, A.C.1    Kirsch, J.F.2
  • 26
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • DOI 10.1006/abio.1996.0238
    • Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase Anal. Biochem. 237, 260-273 (Pubitemid 26177089)
    • (1996) Analytical Biochemistry , vol.237 , Issue.2 , pp. 260-273
    • Kuzmic, P.1
  • 27
    • 0020478357 scopus 로고
    • Adenosine cyclic 3-2,5-2-monophosphate dependent protein kinase: Kinetic mechanism for the bovine skeletal muscle catalytic subunit
    • Cook, P. F., Neville, M. E., Jr., Vrana, K. E., Hartl, F. T., and Roskoski, R., Jr. (1982) Adenosine cyclic 3-2,5-2-monophosphate dependent protein kinase: kinetic mechanism for the bovine skeletal muscle catalytic subunit Biochemistry 21, 5794-5799
    • (1982) Biochemistry , vol.21 , pp. 5794-5799
    • Cook, P.F.1    Neville, Jr.M.E.2    Vrana, K.E.3    Hartl, F.T.4    Roskoski, Jr.R.5
  • 28
    • 0024298850 scopus 로고
    • Isotope partitioning in the adenosine 3-2,5-2-monophosphate dependent protein kinase reaction indicates a steady-state random kinetic mechanism
    • Kong, C. T. and Cook, P. F. (1988) Isotope partitioning in the adenosine 3-2,5-2-monophosphate dependent protein kinase reaction indicates a steady-state random kinetic mechanism Biochemistry 27, 4795-4799
    • (1988) Biochemistry , vol.27 , pp. 4795-4799
    • Kong, C.T.1    Cook, P.F.2
  • 29
    • 77951670691 scopus 로고    scopus 로고
    • Phosphorylation of the transcription factor Ets-1 by ERK2: Rapid dissociation of ADP and phospho-Ets-1
    • Callaway, K., Waas, W. F., Rainey, M. A., Ren, P., and Dalby, K. N. (2010) Phosphorylation of the transcription factor Ets-1 by ERK2: rapid dissociation of ADP and phospho-Ets-1 Biochemistry 49, 3619-3630
    • (2010) Biochemistry , vol.49 , pp. 3619-3630
    • Callaway, K.1    Waas, W.F.2    Rainey, M.A.3    Ren, P.4    Dalby, K.N.5
  • 30
    • 0031444107 scopus 로고    scopus 로고
    • Participation of ADP dissociation in the rate-determining step in cAMP- dependent protein kinase
    • DOI 10.1021/bi971438n
    • Zhou, J. and Adams, J. A. (1997) Participation of ADP dissociation in the rate-determining step in cAMP- dependent protein kinase Biochemistry 36, 15733-15738 (Pubitemid 28027372)
    • (1997) Biochemistry , vol.36 , Issue.50 , pp. 15733-15738
    • Zhou, J.1    Adams, J.A.2
  • 31
    • 0025241896 scopus 로고
    • Ordered multisite protein phosphorylation. Analysis of glycogen synthase kinase 3 action using model peptide substrates
    • Fiol, C. J., Wang, A., Roeske, R. W., and Roach, P. J. (1990) Ordered multisite protein phosphorylation. Analysis of glycogen synthase kinase 3 action using model peptide substrates J. Biol. Chem. 265, 6061-6065
    • (1990) J. Biol. Chem. , vol.265 , pp. 6061-6065
    • Fiol, C.J.1    Wang, A.2    Roeske, R.W.3    Roach, P.J.4
  • 33
    • 3142781362 scopus 로고    scopus 로고
    • Chemical clamping allows for efficient phosphorylation of the RNA carrier protein Np13
    • DOI 10.1074/jbc.M402797200
    • Aubol, B. E., Ungs, L., Lukasiewicz, R., Ghosh, G., and Adams, J. A. (2004) Chemical clamping allows for efficient phosphorylation of the RNA carrier protein Npl3 J. Biol. Chem. 279, 30182-30188 (Pubitemid 38937942)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.29 , pp. 30182-30188
    • Aubol, B.E.1    Ungs, L.2    Lukasiewicz, R.3    Ghosh, G.4    Adams, J.A.5
  • 34
    • 77957754590 scopus 로고    scopus 로고
    • Mechanism of dephosphorylation of the SR protein ASF/SF2 by protein phosphatase 1
    • Ma, C. T., Ghosh, G., Fu, X. D., and Adams, J. A. (2010) Mechanism of dephosphorylation of the SR protein ASF/SF2 by protein phosphatase 1 J. Mol. Biol. 403, 386-404
    • (2010) J. Mol. Biol. , vol.403 , pp. 386-404
    • Ma, C.T.1    Ghosh, G.2    Fu, X.D.3    Adams, J.A.4
  • 35
    • 0033574564 scopus 로고    scopus 로고
    • The subcellular localization of SF2/ASF is regulated by direct interaction with SR protein kinases (SRPKs)
    • Koizumi, J., Okamoto, Y., Onogi, H., Mayeda, A., Krainer, A. R., and 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
    • Koizumi, J.1    Okamoto, Y.2    Onogi, H.3    Mayeda, A.4    Krainer, A.R.5    Hagiwara, M.6
  • 36
    • 0034698665 scopus 로고    scopus 로고
    • Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae
    • Yun, C. Y. and Fu, X. D. (2000) Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae J. Cell Biol. 150, 707-718
    • (2000) J. Cell Biol. , vol.150 , pp. 707-718
    • Yun, C.Y.1    Fu, X.D.2
  • 38
    • 25844491145 scopus 로고    scopus 로고
    • Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2
    • DOI 10.1016/j.molcel.2005.08.025, PII S1097276505015674
    • Ngo, J. C., Chakrabarti, S., Ding, J. H., Velazquez-Dones, A., Nolen, B., Aubol, B. E., Adams, J. A., Fu, X. D., and Ghosh, G. (2005) Interplay between SRPK and Clk/Sty Kinases in Phosphorylation of the Splicing Factor ASF/SF2 Is Regulated by a Docking Motif in ASF/SF2 Mol. Cell 20, 77-89 (Pubitemid 41396564)
    • (2005) Molecular Cell , vol.20 , Issue.1 , pp. 77-89
    • Ngo, J.C.K.1    Chakrabarti, S.2    Ding, J.-H.3    Velazquez-Dones, A.4    Nolen, B.5    Aubol, B.E.6    Adams, J.A.7    Fu, X.-D.8    Ghosh, G.9
  • 41
    • 73149115306 scopus 로고    scopus 로고
    • Allosteric interactions direct binding and phosphorylation of ASF/SF2 by SRPK1
    • Huynh, N., Ma, C. T., Giang, N., Hagopian, J., Ngo, J., Adams, J., and Ghosh, G. (2009) Allosteric interactions direct binding and phosphorylation of ASF/SF2 by SRPK1 Biochemistry 48, 11432-11440
    • (2009) Biochemistry , vol.48 , pp. 11432-11440
    • Huynh, N.1    Ma, C.T.2    Giang, N.3    Hagopian, J.4    Ngo, J.5    Adams, J.6    Ghosh, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.