메뉴 건너뛰기




Volumn 378, Issue 1, 2004, Pages 229-238

SIPP1, a novel pre-mRNa splicing factor and interactor of protein phosphatase-1

Author keywords

Dephosphorylation; Polyglutamine tract; Protein phosphatase 1 (PP1); SIPP1; Spliceosome; Splicing

Indexed keywords

CATALYSIS; ENZYME INHIBITION; FLUORESCENCE; PROTEINS; SEDIMENTATION;

EID: 1542314816     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030950     Document Type: Article
Times cited : (50)

References (42)
  • 1
    • 0035399464 scopus 로고    scopus 로고
    • Combinatorial control of protein phosphatase-1
    • Bollen, M. (2001) Combinatorial control of protein phosphatase-1. Trends Biochem. Sci. 26, 426-431
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 426-431
    • Bollen, M.1
  • 2
    • 0036498531 scopus 로고    scopus 로고
    • Signaling by protein phosphatases in the nucleus
    • Bollen, M. and Beullens, M. (2002) Signaling by protein phosphatases in the nucleus. Trends Cell Biol. 12, 138-145
    • (2002) Trends Cell Biol. , vol.12 , pp. 138-145
    • Bollen, M.1    Beullens, M.2
  • 3
    • 0036010598 scopus 로고    scopus 로고
    • Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution
    • Ceulemans, H., Stalmans, W. and Bollen M. (2002) Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution. BioEssays 24, 371-381
    • (2002) BioEssays , vol.24 , pp. 371-381
    • Ceulemans, H.1    Stalmans, W.2    Bollen, M.3
  • 4
    • 0037081563 scopus 로고    scopus 로고
    • Protein phosphatase 1 - Targeted in many directions
    • Cohen, P. T. W. (2002) Protein phosphatase 1 - targeted in many directions. J. Cell Sci. 115, 241-256
    • (2002) J. Cell Sci. , vol.115 , pp. 241-256
    • Cohen, P.T.W.1
  • 5
    • 0030977268 scopus 로고    scopus 로고
    • Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phophatase 1
    • Egloff, M.-P., Johnson, D. F., Moorhead, G., Cohen, P. T. W., Cohen, P. and Barford, D. (1997) Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phophatase 1. EMBO J. 16, 1876-1887
    • (1997) EMBO J. , vol.16 , pp. 1876-1887
    • Egloff, M.-P.1    Johnson, D.F.2    Moorhead, G.3    Cohen, P.T.W.4    Cohen, P.5    Barford, D.6
  • 6
    • 0030680153 scopus 로고    scopus 로고
    • Targeting of the catalytic subunit of protein phosphatase-1 to the glycolytic enzyme phosphofructokinase
    • Zhao, S. and Lee, E. Y. C. (1997) Targeting of the catalytic subunit of protein phosphatase-1 to the glycolytic enzyme phosphofructokinase. J. Biol. Chem. 272, 28368-28372
    • (1997) J. Biol. Chem. , vol.272 , pp. 28368-28372
    • Zhao, S.1    Lee, E.Y.C.2
  • 7
    • 0038819929 scopus 로고    scopus 로고
    • Degeneracy and function of the ubiquitous RVXF-motif that mediates binding to protein phosphatase-1
    • Wakula, P., Beullens, M., Ceulemans, H., Stalmans, W. and Bollen, M. (2003) Degeneracy and function of the ubiquitous RVXF-motif that mediates binding to protein phosphatase-1. J. Biol. Chem. 278, 18817-18823
    • (2003) J. Biol. Chem. , vol.278 , pp. 18817-18823
    • Wakula, P.1    Beullens, M.2    Ceulemans, H.3    Stalmans, W.4    Bollen, M.5
  • 8
    • 0021840722 scopus 로고
    • The protein phosphatases involved in cellular regulation: Purification and characterisation of the glycogen-bound form of protein phosphatase-1 from rabbit skeletal muscle
    • Stralfors, P., Hiraga, A. and Cohen, P. (1985) The protein phosphatases involved in cellular regulation: purification and characterisation of the glycogen-bound form of protein phosphatase-1 from rabbit skeletal muscle. Eur. J. Biochem. 149, 295-303
    • (1985) Eur. J. Biochem. , vol.149 , pp. 295-303
    • Stralfors, P.1    Hiraga, A.2    Cohen, P.3
  • 9
    • 0026671202 scopus 로고
    • The isolation of novel inhibitory polypeptides of protein phosphatase 1 from bovine thymus nuclei
    • Beullens, M., Van Eynde, A., Stalmans, W. and Bollen, M. (1992) The isolation of novel inhibitory polypeptides of protein phosphatase 1 from bovine thymus nuclei. J. Biol. Chem. 267, 16538-16544
    • (1992) J. Biol. Chem. , vol.267 , pp. 16538-16544
    • Beullens, M.1    Van Eynde, A.2    Stalmans, W.3    Bollen, M.4
  • 10
    • 0027049145 scopus 로고
    • The control of protein phosphatase-1 by targetting subunits: The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1
    • Alessi, D., MacDougall, L. K., Sola, M. M., Ikebe, M. and Cohen, P. (1992) The control of protein phosphatase-1 by targetting subunits: the major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. Eur. J. Biochem. 210, 1023-1035
    • (1992) Eur. J. Biochem. , vol.210 , pp. 1023-1035
    • Alessi, D.1    MacDougall, L.K.2    Sola, M.M.3    Ikebe, M.4    Cohen, P.5
  • 11
    • 0029952112 scopus 로고    scopus 로고
    • Identification of protein phosphatase-1-binding proteins by microcystin-biotin affinity chromatography
    • Campos, M., Fadden, P., Alms, G., Qian, Z. and Haystead, T. A. J. (1996) Identification of protein phosphatase-1-binding proteins by microcystin-biotin affinity chromatography. J. Biol. Chem. 271, 28478-28484
    • (1996) J. Biol. Chem. , vol.271 , pp. 28478-28484
    • Campos, M.1    Fadden, P.2    Alms, G.3    Qian, Z.4    Haystead, T.A.J.5
  • 12
    • 0037133234 scopus 로고    scopus 로고
    • Novel interactions of Saccharomyces cerevisiae type 1 protein phosphatase identified by single-step affinity purification and mass spectrometry
    • Walsh, E. P., Lamont, D. J., Beattie, K. A. and Stark, M. J. (2002) Novel interactions of Saccharomyces cerevisiae type 1 protein phosphatase identified by single-step affinity purification and mass spectrometry. Biochemistry 41, 2409-2420
    • (2002) Biochemistry , vol.41 , pp. 2409-2420
    • Walsh, E.P.1    Lamont, D.J.2    Beattie, K.A.3    Stark, M.J.4
  • 13
    • 0037033022 scopus 로고    scopus 로고
    • Binding of the concave surface of the Sds22 superhelix to the α4/α5/α6-triangle of protein phosphatase-1
    • Ceulemans, H., Vulsteke, V., De Maeyer, M., Tatchell, K., Stalmans, W. and Bollen, M. (2002) Binding of the concave surface of the Sds22 superhelix to the α4/α5/α6-triangle of protein phosphatase-1. J. Biol. Chem. 277, 47331-47337
    • (2002) J. Biol. Chem. , vol.277 , pp. 47331-47337
    • Ceulemans, H.1    Vulsteke, V.2    De Maeyer, M.3    Tatchell, K.4    Stalmans, W.5    Bollen, M.6
  • 14
    • 0029617851 scopus 로고
    • Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour suppressor p53
    • Helps, N. R., Barker, H. M., Elledge, S. J. and Cohen, P. T. W. (1995) Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour suppressor p53. FEBS Lett. 377, 295-300
    • (1995) FEBS Lett. , vol.377 , pp. 295-300
    • Helps, N.R.1    Barker, H.M.2    Elledge, S.J.3    Cohen, P.T.W.4
  • 15
    • 0032969182 scopus 로고    scopus 로고
    • Interactions of protein phosphatase type 1, with a focus on myosin phosphatase
    • Hartshorne, D. J. and Hirano, K. (1999) Interactions of protein phosphatase type 1, with a focus on myosin phosphatase. Mol. Cell. Biochem. 190, 79-84
    • (1999) Mol. Cell. Biochem. , vol.190 , pp. 79-84
    • Hartshorne, D.J.1    Hirano, K.2
  • 17
    • 0037223607 scopus 로고    scopus 로고
    • Trithorax interacts with type 1 serine/threonine protein phosphatase in Drosophila
    • Rudenko, A., Bennett, D. and Alphey, L. (2003) Trithorax interacts with type 1 serine/threonine protein phosphatase in Drosophila. EMBO Rep. 4, 59-63
    • (2003) EMBO Rep. , vol.4 , pp. 59-63
    • Rudenko, A.1    Bennett, D.2    Alphey, L.3
  • 18
    • 0033579540 scopus 로고    scopus 로고
    • Association of two nuclear proteins, Npw38 and NpwBP, via the interaction between the WW domain and a novel proline-rich motif containing glycine and arginine
    • Komuro, A., Saeki, M. and Kato, S. (1999) Association of two nuclear proteins, Npw38 and NpwBP, via the interaction between the WW domain and a novel proline-rich motif containing glycine and arginine. J. Biol. Chem. 274, 36513-36519
    • (1999) J. Biol. Chem. , vol.274 , pp. 36513-36519
    • Komuro, A.1    Saeki, M.2    Kato, S.3
  • 19
    • 0035839612 scopus 로고    scopus 로고
    • A nuclear SH3 domain-binding protein that colocalizes with mRNA splicing factors and intermediate filament-containing perinuclear networks
    • Craggs, G., Finan, P. M., Lawson, D., Wingfield, J., Perera, T., Gadher, S., Totty, N. F. and Kellie, S. (2001) A nuclear SH3 domain-binding protein that colocalizes with mRNA splicing factors and intermediate filament-containing perinuclear networks. J. Biol. Chem. 276, 30552-30560
    • (2001) J. Biol. Chem. , vol.276 , pp. 30552-30560
    • Craggs, G.1    Finan, P.M.2    Lawson, D.3    Wingfield, J.4    Perera, T.5    Gadher, S.6    Totty, N.F.7    Kellie, S.8
  • 20
    • 0023780669 scopus 로고
    • Preparation of low-molecular-weight forms of rabbit muscle protein phosphatase
    • DeGuzman, A. and Lee, E. Y. C. (1988) Preparation of low-molecular- weight forms of rabbit muscle protein phosphatase. Methods Enzymol. 159, 356-368
    • (1988) Methods Enzymol. , vol.159 , pp. 356-368
    • DeGuzman, A.1    Lee, E.Y.C.2
  • 21
    • 0031019156 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis of protein phosphatase type 1 in the yeast Saccharomyces cerevisiae
    • Baker, S. H., Frederick, D. L., Bloecher, A. and Tatchell, K. (1997) Alanine-scanning mutagenesis of protein phosphatase type 1 in the yeast Saccharomyces cerevisiae. Genetics 145, 615-626
    • (1997) Genetics , vol.145 , pp. 615-626
    • Baker, S.H.1    Frederick, D.L.2    Bloecher, A.3    Tatchell, K.4
  • 22
    • 0030698842 scopus 로고    scopus 로고
    • Stable DNA-binding yeast vector allowing high-bait expression for use in the two-hybrid system
    • Louvet, O., Doignon, F. and Crouzet, M. (1997) Stable DNA-binding yeast vector allowing high-bait expression for use in the two-hybrid system. BioTechniques 23, 816-818, 820
    • (1997) BioTechniques , vol.23 , pp. 816-818
    • Louvet, O.1    Doignon, F.2    Crouzet, M.3
  • 23
    • 0028145447 scopus 로고
    • Signaling through transforming G protein-coupled receptors in NIH 3T3 cells involves c-Raf activation: Evidence for a protein kinase C-independent pathway
    • Crespo, P., Xu, N., Daniotti, J. L., Troppmair, J., Rapp, U. R. and Gutkind, J. S. (1994) Signaling through transforming G protein-coupled receptors in NIH 3T3 cells involves c-Raf activation: evidence for a protein kinase C-independent pathway J. Biol. Chem. 269, 21103-21109
    • (1994) J. Biol. Chem. , vol.269 , pp. 21103-21109
    • Crespo, P.1    Xu, N.2    Daniotti, J.L.3    Troppmair, J.4    Rapp, U.R.5    Gutkind, J.S.6
  • 24
    • 0031603686 scopus 로고    scopus 로고
    • The isolation of novel inhibitory polypeptides of protein phosphatase 1 from bovine thymus nuclei
    • Beullens, M., Stalmans, W. and Bollen, M. (1998) The isolation of novel inhibitory polypeptides of protein phosphatase 1 from bovine thymus nuclei. Methods Mol. Biol. 93, 145-155
    • (1998) Methods Mol. Biol. , vol.93 , pp. 145-155
    • Beullens, M.1    Stalmans, W.2    Bollen, M.3
  • 25
    • 0037205485 scopus 로고    scopus 로고
    • The protein phosphatase-1 regulator NIPP1 is also a splicing factor involved in a late step of spliceosome assembly
    • Beullens, M. and Bollen, M. (2002) The protein phosphatase-1 regulator NIPP1 is also a splicing factor involved in a late step of spliceosome assembly. J. Biol. Chem. 277, 19885-19860
    • (2002) J. Biol. Chem. , vol.277 , pp. 19885-119860
    • Beullens, M.1    Bollen, M.2
  • 26
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • Egloff, M.-P., Cohen, P. T. W., Reinemer, P. and Barford, D. (1995) Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J. Mol. Biol. 254, 942-959
    • (1995) J. Mol. Biol. , vol.254 , pp. 942-959
    • Egloff, M.-P.1    Cohen, P.T.W.2    Reinemer, P.3    Barford, D.4
  • 27
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg, J., Huang, H., Kwon, Y., Greengard, P., Nairn, A. C. and Kuriyan, J. (1995) Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature (London) 376, 745-753
    • (1995) Nature (London) , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.2    Kwon, Y.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 28
    • 0031128181 scopus 로고    scopus 로고
    • Protein phosphorylation and the nuclear organization of pre-mRNA splicing
    • Misteli, T. and Spector, D. L. (1997) Protein phosphorylation and the nuclear organization of pre-mRNA splicing. Trends Cell Biol. 7, 135-138
    • (1997) Trends Cell Biol. , vol.7 , pp. 135-138
    • Misteli, T.1    Spector, D.L.2
  • 29
    • 0028043718 scopus 로고
    • Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism
    • Mermoud, J. E., Cohen, P. T. and Lamond, A. I. (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
  • 30
    • 0035824660 scopus 로고    scopus 로고
    • Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle
    • Katayama, H., Zhou, H., Li, Q., Tatsuka, M. and Sen, S. (2001) Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle. J. Biol. Chem. 276, 46219-46224
    • (2001) J. Biol. Chem. , vol.276 , pp. 46219-46224
    • Katayama, H.1    Zhou, H.2    Li, Q.3    Tatsuka, M.4    Sen, S.5
  • 31
    • 0034808081 scopus 로고    scopus 로고
    • Growth arrest and DNa damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1
    • Connor, J. H., Weiser, D. C., Li, S., Hallenbeck, J. M. and Shenolikar, S. (2001) Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Mol. Cell. Biol. 21, 6841-6850
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6841-6850
    • Connor, J.H.1    Weiser, D.C.2    Li, S.3    Hallenbeck, J.M.4    Shenolikar, S.5
  • 32
    • 1542382700 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 33
    • 1542322696 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 35
    • 0034680311 scopus 로고    scopus 로고
    • Evidence that dim1 associates with proteins involved in pre-mRNA splicing and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1
    • Zhang, Y-Z., Lindblom, T., Chang, A., Sudol, M., Sluder, A. E. and Golemis, E. A. (2000) Evidence that dim1 associates with proteins involved in pre-mRNA splicing and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1. Gene 257, 33-43
    • (2000) Gene , vol.257 , pp. 33-43
    • Zhang, Y.-Z.1    Lindblom, T.2    Chang, A.3    Sudol, M.4    Sluder, A.E.5    Golemis, E.A.6
  • 36
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • Zhou, Z., Licklider, L. J., Gygi, S. P. and Reed, R. (2002) Comprehensive proteomic analysis of the human spliceosome. Nature (London) 419, 182-185
    • (2002) Nature (London) , vol.419 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4
  • 37
    • 1542382701 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 38
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • Macias, M. J., Wiesner, S. and Sudol, M. (2002) WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Lett. 513, 30-37
    • (2002) FEBS Lett. , vol.513 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 42
    • 0037200062 scopus 로고    scopus 로고
    • Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1
    • Boudrez, A., Beullens, M., Waelkens, E., Stalmans, W. and Bollen, M. (2002) Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1. J. Biol. Chem. 277, 31834-31841
    • (2002) J. Biol. Chem. , vol.277 , pp. 31834-31841
    • Boudrez, A.1    Beullens, M.2    Waelkens, E.3    Stalmans, W.4    Bollen, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.