메뉴 건너뛰기




Volumn 581, Issue 2, 2007, Pages 223-232

Phosphorylation by SR kinases regulates the binding of PTB-associated splicing factor (PSF) to the pre-mRNA polypyrimidine tract

Author keywords

Phosphorylation; Ribonucleoprotein; snRNA; Spliceosome

Indexed keywords

EPITOPE; MESSENGER RNA PRECURSOR; MONOCLONAL ANTIBODY; PROTEIN KINASE; PROTEIN PSF; PROTEIN SERINE ARGININE KINASE; PYRIMIDINE; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG;

EID: 33846268431     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.12.015     Document Type: Article
Times cited : (21)

References (56)
  • 1
    • 0029891101 scopus 로고    scopus 로고
    • The structure and function of proteins involved in mammalian pre-mRNA splicing
    • Kramer A. The structure and function of proteins involved in mammalian pre-mRNA splicing. Annu. Rev. Biochem. 65 (1996) 367-409
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 367-409
    • Kramer, A.1
  • 2
    • 0032489021 scopus 로고    scopus 로고
    • Mechanical devices of the spliceosome: motors, clocks, springs, and things
    • Staley J.P., and Guthrie C. Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell 92 (1998) 315-326
    • (1998) Cell , vol.92 , pp. 315-326
    • Staley, J.P.1    Guthrie, C.2
  • 3
    • 0030595187 scopus 로고    scopus 로고
    • Interaction of U2AF65 RS region with pre-mRNA branch point and promotion of base pairing with U2 snRNA
    • Valcarcel J., Gaur R.K., Singh R., and Green M.R. Interaction of U2AF65 RS region with pre-mRNA branch point and promotion of base pairing with U2 snRNA. Science 273 (1996) 1706-1709
    • (1996) Science , vol.273 , pp. 1706-1709
    • Valcarcel, J.1    Gaur, R.K.2    Singh, R.3    Green, M.R.4
  • 4
    • 0029372979 scopus 로고
    • The superfamily of arginine/serine-rich splicing factors
    • Fu X.D. The superfamily of arginine/serine-rich splicing factors. RNA 1 (1995) 663-680
    • (1995) RNA , vol.1 , pp. 663-680
    • Fu, X.D.1
  • 5
    • 0025856790 scopus 로고
    • Characterization and molecular cloning of polypyrimidine tract-binding protein: a component of a complex necessary for pre-mRNA splicing
    • Patton J.G., Mayer S.A., Tempst P., and Nadal-Ginard B. Characterization and molecular cloning of polypyrimidine tract-binding protein: a component of a complex necessary for pre-mRNA splicing. Genes Dev. 5 (1991) 1237-1251
    • (1991) Genes Dev. , vol.5 , pp. 1237-1251
    • Patton, J.G.1    Mayer, S.A.2    Tempst, P.3    Nadal-Ginard, B.4
  • 7
    • 0037032415 scopus 로고    scopus 로고
    • PSF and p54(nrb)/NonO-multi-functional nuclear proteins
    • Shav-Tal Y., and Zipori D. PSF and p54(nrb)/NonO-multi-functional nuclear proteins. FEBS Lett. 531 (2002) 109-114
    • (2002) FEBS Lett. , vol.531 , pp. 109-114
    • Shav-Tal, Y.1    Zipori, D.2
  • 8
    • 0027401652 scopus 로고
    • Purification and characterization of a DNA-binding heterodimer of 52 and 100 kDa from HeLa cells
    • Zhang W.W., Zhang L.X., Busch R.K., Farres J., and Busch H. Purification and characterization of a DNA-binding heterodimer of 52 and 100 kDa from HeLa cells. Biochem. J. 290 (1993) 267-272
    • (1993) Biochem. J. , vol.290 , pp. 267-272
    • Zhang, W.W.1    Zhang, L.X.2    Busch, R.K.3    Farres, J.4    Busch, H.5
  • 9
    • 0027305376 scopus 로고
    • nrb, a nuclear protein with two RNA recognition motifs and extensive homology to human splicing factor PSF and Drosophila NONA/BJ6
    • nrb, a nuclear protein with two RNA recognition motifs and extensive homology to human splicing factor PSF and Drosophila NONA/BJ6. Nucleic Acids Res. 21 (1993) 4085-4092
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4085-4092
    • Dong, B.1    Horowitz, D.S.2    Kobayashi, R.3    Krainer, A.R.4
  • 11
    • 0142011032 scopus 로고    scopus 로고
    • The Hrp65 self interaction is mediated by an evolutionarily conserved domain and is required for nuclear import of Hrp65 isoforms that lack a nuclear localization signal
    • Kiesler E., Miralles F., Ostlund Farrants A.K., and Visa N. The Hrp65 self interaction is mediated by an evolutionarily conserved domain and is required for nuclear import of Hrp65 isoforms that lack a nuclear localization signal. J. Cell Sci. 116 (2003) 3949-3956
    • (2003) J. Cell Sci. , vol.116 , pp. 3949-3956
    • Kiesler, E.1    Miralles, F.2    Ostlund Farrants, A.K.3    Visa, N.4
  • 13
    • 0030696683 scopus 로고    scopus 로고
    • The human U5 snRNP-specific 100-kD protein is an RS domain containing, putative RNA helicase with significant homology to the yeast splicing factor Prp28
    • Teigelkamp S., Mundt C., Achsel T., Will C.L., and Luhrmann R. The human U5 snRNP-specific 100-kD protein is an RS domain containing, putative RNA helicase with significant homology to the yeast splicing factor Prp28. RNA 3 (1997) 1313-1326
    • (1997) RNA , vol.3 , pp. 1313-1326
    • Teigelkamp, S.1    Mundt, C.2    Achsel, T.3    Will, C.L.4    Luhrmann, R.5
  • 14
    • 0028360767 scopus 로고
    • A novel set of spliceosome-associated proteins and the essential splicing factor PSF bind stably to pre-mRNA prior to catalytic step II of the splicing reaction
    • Gozani O., Patton J.G., and Reed R. A novel set of spliceosome-associated proteins and the essential splicing factor PSF bind stably to pre-mRNA prior to catalytic step II of the splicing reaction. EMBO J. 13 (1994) 3356-3367
    • (1994) EMBO J. , vol.13 , pp. 3356-3367
    • Gozani, O.1    Patton, J.G.2    Reed, R.3
  • 15
    • 0037041395 scopus 로고    scopus 로고
    • An extensive network of coupling among gene expression machines
    • Maniatis T., and Reed R. An extensive network of coupling among gene expression machines. Nature 416 (2002) 499-506
    • (2002) Nature , vol.416 , pp. 499-506
    • Maniatis, T.1    Reed, R.2
  • 16
    • 0036715543 scopus 로고    scopus 로고
    • Splicing and transcription-associated proteins PSF and p54nrb/nonO bind to the RNA polymerase II CTD
    • Emili A., Shales M., McCracken S., Xie W., Tucker P.W., Kobayashi R., Blencowe B.J., and Ingles C.J. Splicing and transcription-associated proteins PSF and p54nrb/nonO bind to the RNA polymerase II CTD. RNA 8 (2002) 1102-1111
    • (2002) RNA , vol.8 , pp. 1102-1111
    • Emili, A.1    Shales, M.2    McCracken, S.3    Xie, W.4    Tucker, P.W.5    Kobayashi, R.6    Blencowe, B.J.7    Ingles, C.J.8
  • 17
    • 0242384920 scopus 로고    scopus 로고
    • Transcriptional activators control splicing and 3′-end cleavage levels
    • Rosonina E., Bakowski M.A., McCracken S., and Blencowe B.J. Transcriptional activators control splicing and 3′-end cleavage levels. J. Biol. Chem. 278 (2003) 43034-43040
    • (2003) J. Biol. Chem. , vol.278 , pp. 43034-43040
    • Rosonina, E.1    Bakowski, M.A.2    McCracken, S.3    Blencowe, B.J.4
  • 19
    • 0035106562 scopus 로고    scopus 로고
    • PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors
    • Mathur M., Tucker P.W., and Samuels H.H. PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors. Mol. Cell. Biol. 21 (2001) 2298-2311
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2298-2311
    • Mathur, M.1    Tucker, P.W.2    Samuels, H.H.3
  • 20
    • 0036212259 scopus 로고    scopus 로고
    • Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription
    • Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N., and Waterman M.R. Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription. Endocrinology 143 (2002) 1280-1290
    • (2002) Endocrinology , vol.143 , pp. 1280-1290
    • Sewer, M.B.1    Nguyen, V.Q.2    Huang, C.J.3    Tucker, P.W.4    Kagawa, N.5    Waterman, M.R.6
  • 21
    • 14044257206 scopus 로고    scopus 로고
    • Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor
    • Bladen C.L., Udayakumar D., Takeda Y., and Dynan W.S. Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor. J. Biol. Chem. 280 (2005) 5205-5210
    • (2005) J. Biol. Chem. , vol.280 , pp. 5205-5210
    • Bladen, C.L.1    Udayakumar, D.2    Takeda, Y.3    Dynan, W.S.4
  • 22
    • 0035943347 scopus 로고    scopus 로고
    • The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs
    • Zhang Z., and Carmichael G.G. The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs. Cell 106 (2001) 465-475
    • (2001) Cell , vol.106 , pp. 465-475
    • Zhang, Z.1    Carmichael, G.G.2
  • 24
    • 0029744344 scopus 로고    scopus 로고
    • SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors
    • Colwill K., Feng L.L., Yeakley J.M., Gish G.D., Caceres J.F., Pawson T., and Fu X.D. SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors. J. Biol. Chem. 271 (1996) 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
  • 26
    • 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. Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae. J. Cell Biol. 150 (2000) 707-718
    • (2000) J. Cell Biol. , vol.150 , pp. 707-718
    • Yun, C.Y.1    Fu, X.D.2
  • 27
    • 0035260659 scopus 로고    scopus 로고
    • Phosphorylation by Sky1p promotes Npl3p shuttling and mRNA dissociation
    • Gilbert W., Siebel C.W., and Guthrie C. Phosphorylation by Sky1p promotes Npl3p shuttling and mRNA dissociation. RNA 7 (2001) 302-313
    • (2001) RNA , vol.7 , pp. 302-313
    • Gilbert, W.1    Siebel, C.W.2    Guthrie, C.3
  • 28
    • 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., Lin W., Dyck J.A., Yeakley J.M., Songyang Z., Cantley L.C., and Fu X.D. 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 (1998) 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
  • 29
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley B.R. Sorting out the complexity of SR protein functions. RNA 6 (2000) 1197-1211
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 30
    • 14744290800 scopus 로고    scopus 로고
    • RS domains contact the pre-mRNA throughout spliceosome assembly
    • Hertel K.J., and Graveley B.R. RS domains contact the pre-mRNA throughout spliceosome assembly. Trends Biochem. Sci. 30 (2005) 115-118
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 115-118
    • Hertel, K.J.1    Graveley, B.R.2
  • 31
    • 8644268780 scopus 로고    scopus 로고
    • A pathway of sequential arginine-serine-rich domain splicing signal interactions during mammalian spliceosome assembly
    • Shen H., and Green M.R. A pathway of sequential arginine-serine-rich domain splicing signal interactions during mammalian spliceosome assembly. Mol. Cell 16 (2004) 363-373
    • (2004) Mol. Cell , vol.16 , pp. 363-373
    • Shen, H.1    Green, M.R.2
  • 32
    • 1242316952 scopus 로고    scopus 로고
    • Arginine-serine-rich domains bound at splicing enhancers contact the branchpoint to promote pre-spliceosome assembly
    • Shen H., Kan J.L., and Green M.R. Arginine-serine-rich domains bound at splicing enhancers contact the branchpoint to promote pre-spliceosome assembly. Mol. Cell 13 (2004) 367-376
    • (2004) Mol. Cell , vol.13 , pp. 367-376
    • Shen, H.1    Kan, J.L.2    Green, M.R.3
  • 33
    • 0030610392 scopus 로고    scopus 로고
    • The [U4/U6.U5] tri-snRNP-specific 27K protein is a novel SR protein that can be phosphorylated by the snRNP-associated protein kinase
    • Fetzer S., Lauber J., Will C.L., and Luhrmann R. The [U4/U6.U5] tri-snRNP-specific 27K protein is a novel SR protein that can be phosphorylated by the snRNP-associated protein kinase. RNA 3 (1997) 344-355
    • (1997) RNA , vol.3 , pp. 344-355
    • Fetzer, S.1    Lauber, J.2    Will, C.L.3    Luhrmann, R.4
  • 34
    • 0029377886 scopus 로고
    • SR proteins escort the U4/U6.U5 tri-snRNP to the spliceosome
    • Roscigno R.F., and Garcia-Blanco M.A. SR proteins escort the U4/U6.U5 tri-snRNP to the spliceosome. RNA 1 (1995) 692-706
    • (1995) RNA , vol.1 , pp. 692-706
    • Roscigno, R.F.1    Garcia-Blanco, M.A.2
  • 35
    • 16244399185 scopus 로고    scopus 로고
    • A novel SR-related protein is required for the second step of pre-mRNA splicing
    • Cazalla D., Newton K., and Caceres J.F. A novel SR-related protein is required for the second step of pre-mRNA splicing. Mol. Cell. Biol. 25 (2005) 2969-2980
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2969-2980
    • Cazalla, D.1    Newton, K.2    Caceres, J.F.3
  • 36
    • 14644445227 scopus 로고    scopus 로고
    • SRprises along a messenger's journey
    • Huang Y., and Steitz J.A. SRprises along a messenger's journey. Mol. Cell 17 (2005) 613-615
    • (2005) Mol. Cell , vol.17 , pp. 613-615
    • Huang, Y.1    Steitz, J.A.2
  • 37
    • 0034823538 scopus 로고    scopus 로고
    • Identification of tyrosine phosphorylated proteins associated with the nuclear envelope
    • Otto H., Dreger M., Bengtsson L., and Hucho F. Identification of tyrosine phosphorylated proteins associated with the nuclear envelope. Euro. J. Biochem. 268 (2001) 420-428
    • (2001) Euro. J. Biochem. , vol.268 , pp. 420-428
    • Otto, H.1    Dreger, M.2    Bengtsson, L.3    Hucho, F.4
  • 38
    • 0034663495 scopus 로고    scopus 로고
    • Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion
    • Akhmedov A.T., and Lopez B.S. Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion. Nucleic Acids Res. 28 (2000) 3022-3030
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3022-3030
    • Akhmedov, A.T.1    Lopez, B.S.2
  • 39
    • 0030774839 scopus 로고    scopus 로고
    • The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain
    • Deloulme J.C., Prichard L., Delattre O., and Storm D.R. The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain. J. Biol. Chem. 272 (1997) 27369-27377
    • (1997) J. Biol. Chem. , vol.272 , pp. 27369-27377
    • Deloulme, J.C.1    Prichard, L.2    Delattre, O.3    Storm, D.R.4
  • 40
    • 0035159666 scopus 로고    scopus 로고
    • Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions
    • Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G., Vandekerckhove J., and Zipori D. Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions. Mol. Biol. Cell. 12 (2001) 2328-2340
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 2328-2340
    • Shav-Tal, Y.1    Cohen, M.2    Lapter, S.3    Dye, B.4    Patton, J.G.5    Vandekerckhove, J.6    Zipori, D.7
  • 41
    • 0032489442 scopus 로고    scopus 로고
    • Fission yeast mitotic regulator Dsk1 is an SR protein-specific kinase
    • Tang Z., Yanagida M., and Lin R.J. Fission yeast mitotic regulator Dsk1 is an SR protein-specific kinase. J. Biol. Chem. 273 (1998) 5963-5969
    • (1998) J. Biol. Chem. , vol.273 , pp. 5963-5969
    • Tang, Z.1    Yanagida, M.2    Lin, R.J.3
  • 42
    • 0030938085 scopus 로고    scopus 로고
    • Coexpression of nuclear receptor partners increases their solubility and biological activities
    • Li C., Schwabe J.R., Banayo E., and Evans R.M. Coexpression of nuclear receptor partners increases their solubility and biological activities. Proc. Natl. Acad. Sci. 94 (1997) 2278-2283
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 2278-2283
    • Li, C.1    Schwabe, J.R.2    Banayo, E.3    Evans, R.M.4
  • 43
    • 0034146376 scopus 로고    scopus 로고
    • Functional coexpression of serine protein kinase SRPK1 and its substrate ASF/SF2 in Escherichia coli
    • Yue B.G., Ajuh P., Akusjärvi G., Lamond A.I., and Kreivi J.P. Functional coexpression of serine protein kinase SRPK1 and its substrate ASF/SF2 in Escherichia coli. Nucleic Acids Res. 28 (2000) e14
    • (2000) Nucleic Acids Res. , vol.28
    • Yue, B.G.1    Ajuh, P.2    Akusjärvi, G.3    Lamond, A.I.4    Kreivi, J.P.5
  • 45
    • 0022415556 scopus 로고
    • Characterization of a family of nuclear and chromosomal proteins identified by a monoclonal antibody
    • Turner B.M., Davies S., and Whitfield W.G. Characterization of a family of nuclear and chromosomal proteins identified by a monoclonal antibody. Euro. Cell Biol. 38 (1985) 344-352
    • (1985) Euro. Cell Biol. , vol.38 , pp. 344-352
    • Turner, B.M.1    Davies, S.2    Whitfield, W.G.3
  • 46
    • 0026716104 scopus 로고
    • SR proteins: a conserved family of pre-mRNA splicing factors
    • Zahler A.M., Lane W.S., Stolk J.A., and Roth M.B. SR proteins: a conserved family of pre-mRNA splicing factors. Genes Dev. 6 (1992) 837-847
    • (1992) Genes Dev. , vol.6 , pp. 837-847
    • Zahler, A.M.1    Lane, W.S.2    Stolk, J.A.3    Roth, M.B.4
  • 47
    • 0032521186 scopus 로고    scopus 로고
    • A cooperative interaction between U2AF65 and mBBP/SF1 facilitates branchpoint region recognition
    • Berglund J.A., Abovich N., and Rosbash M. A cooperative interaction between U2AF65 and mBBP/SF1 facilitates branchpoint region recognition. Genes Dev. 12 (1998) 858-867
    • (1998) Genes Dev. , vol.12 , pp. 858-867
    • Berglund, J.A.1    Abovich, N.2    Rosbash, M.3
  • 48
    • 2442435550 scopus 로고    scopus 로고
    • p54(nrb) associates with the 5′ splice site within large transcription/splicing complexes
    • Kameoka S., Duque P., and Konarska M.M. p54(nrb) associates with the 5′ splice site within large transcription/splicing complexes. EMBO J. 23 (2004) 1782-1791
    • (2004) EMBO J. , vol.23 , pp. 1782-1791
    • Kameoka, S.1    Duque, P.2    Konarska, M.M.3
  • 49
    • 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., Chen Y., and Manley J.L. Sequence-specific RNA binding by an SR protein requires RS domain phosphorylation: creation of an SRp40-specific splicing enhancer. Proc. Natl. Acad. Sci. 94 (1997) 1148-1153
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 1148-1153
    • Tacke, R.1    Chen, Y.2    Manley, J.L.3
  • 50
    • 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 Manley J.L. Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing. Genes Dev. 11 (1997) 334-344
    • (1997) Genes Dev. , vol.11 , pp. 334-344
    • Xiao, S.H.1    Manley, J.L.2
  • 51
    • 3042836378 scopus 로고    scopus 로고
    • A molecular link between SR protein dephosphorylation and mRNA export
    • Huang Y., Yario T.A., and Steitz J.A. A molecular link between SR protein dephosphorylation and mRNA export. Proc. Natl. Acad. Sci. 101 (2004) 9666-9670
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 9666-9670
    • Huang, Y.1    Yario, T.A.2    Steitz, J.A.3
  • 52
    • 0031468240 scopus 로고    scopus 로고
    • Both phosphorylation and dephosphorylation of ASF/SF2 are required for pre-mRNA splicing in vitro
    • Cao W., Jamison S.F., and Garcia-Blanco M.A. Both phosphorylation and dephosphorylation of ASF/SF2 are required for pre-mRNA splicing in vitro. RNA 3 (1997) 1456-1467
    • (1997) RNA , vol.3 , pp. 1456-1467
    • Cao, W.1    Jamison, S.F.2    Garcia-Blanco, M.A.3
  • 53
    • 0032827418 scopus 로고    scopus 로고
    • The protein kinase Clk/Sty directly modulates SR protein activity: both hyper-and hypophosphorylation inhibit splicing
    • Prasad J., Colwill K., Pawson T., and Manley J.L. The protein kinase Clk/Sty directly modulates SR protein activity: both hyper-and hypophosphorylation inhibit splicing. Mol. Cell. Biol. 19 (1999) 6991-7000
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6991-7000
    • Prasad, J.1    Colwill, K.2    Pawson, T.3    Manley, J.L.4
  • 54
    • 0032476604 scopus 로고    scopus 로고
    • Phosphorylation-dephosphorylation differentially affects activities of splicing factor ASF/SF2
    • Xiao S., and Manley J.L. Phosphorylation-dephosphorylation differentially affects activities of splicing factor ASF/SF2. EMBO J. 17 (1998) 6359-6367
    • (1998) EMBO J. , vol.17 , pp. 6359-6367
    • Xiao, S.1    Manley, J.L.2
  • 55
    • 0030199521 scopus 로고    scopus 로고
    • Interaction of protein phosphatase type 1 with a splicing factor
    • Hirano K., Edodi F., Patton J.G., and Hartshorne D.J. Interaction of protein phosphatase type 1 with a splicing factor. FEBS Lett. 389 (1996) 191-194
    • (1996) FEBS Lett. , vol.389 , pp. 191-194
    • Hirano, K.1    Edodi, F.2    Patton, J.G.3    Hartshorne, D.J.4
  • 56
    • 0032238550 scopus 로고    scopus 로고
    • Protein phosphorylation plays an essential role in the regulation of alternative splicing and sex determination in Drosophila
    • Du C., McGuffin M.E., Dauwalder B., Rabinow L., and Mattox W. Protein phosphorylation plays an essential role in the regulation of alternative splicing and sex determination in Drosophila. Mol. Cell 2 (1998) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.