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Volumn 19, Issue 6, 1999, Pages 4113-4120

pICln inhibits snRNP biogenesis by binding core spliceosomal proteins

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; SMALL NUCLEAR RIBONUCLEOPROTEIN;

EID: 0033018469     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.6.4113     Document Type: Article
Times cited : (89)

References (36)
  • 1
    • 0030614446 scopus 로고    scopus 로고
    • Expression of human pICln and CIC-6 in Xenopus oocytes induces an identical endogenous chloride conductance
    • Buyse, G., T. Voets, J. Tytgat, C. Degreef, G. Droogmans, B. Nilius, and J. Eggermont. 1997. Expression of human pICln and CIC-6 in Xenopus oocytes induces an identical endogenous chloride conductance. J. Biol. Chem. 272: 3615-3621.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3615-3621
    • Buyse, G.1    Voets, T.2    Tytgat, J.3    Degreef, C.4    Droogmans, G.5    Nilius, B.6    Eggermont, J.7
  • 2
    • 0031801378 scopus 로고    scopus 로고
    • The list of potential volume-sensitive chloride channels continues to swell (and shrink)
    • Clapham, D. E. 1998. The list of potential volume-sensitive chloride channels continues to swell (and shrink). J. Gen. Physiol. 111:623-624.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 623-624
    • Clapham, D.E.1
  • 3
    • 0020960311 scopus 로고
    • Nucleocytoplasmic segregation of proteins and RNAs
    • DeRobertis, E. M. 1983. Nucleocytoplasmic segregation of proteins and RNAs. Cell 32:1021-1025.
    • (1983) Cell , vol.32 , pp. 1021-1025
    • DeRobertis, E.M.1
  • 4
    • 0027396947 scopus 로고
    • Nucleo-cytoplasmic transport of U snRNPs: Definition of a nuclear location signal in the Sm core domain that binds a transport receptor independently of the m3G cap
    • Fischer, U., V. Sumpter, M. Sekine, T. Satoh, and R. Luhrmann. 1993. Nucleo-cytoplasmic transport of U snRNPs: definition of a nuclear location signal in the Sm core domain that binds a transport receptor independently of the m3G cap. EMBO J. 12:573-583.
    • (1993) EMBO J. , vol.12 , pp. 573-583
    • Fischer, U.1    Sumpter, V.2    Sekine, M.3    Satoh, T.4    Luhrmann, R.5
  • 5
    • 0030928716 scopus 로고    scopus 로고
    • The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis
    • Fischer, U., Q. Liu, and G. Dreyfuss. 1997. The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis. Cell 90:1023-1029.
    • (1997) Cell , vol.90 , pp. 1023-1029
    • Fischer, U.1    Liu, Q.2    Dreyfuss, G.3
  • 6
    • 0022133408 scopus 로고
    • Small nuclear ribonucleoprotein particle assembly in vivo: Demonstration of a 6S RNA-free core precursor and posttranslational modification
    • Fisher, D. E., G. E. Conner, W. H. Reeves, R. Wisniewolski, and G. Blobel. 1985. Small nuclear ribonucleoprotein particle assembly in vivo: demonstration of a 6S RNA-free core precursor and posttranslational modification. Cell 42:751-758.
    • (1985) Cell , vol.42 , pp. 751-758
    • Fisher, D.E.1    Conner, G.E.2    Reeves, W.H.3    Wisniewolski, R.4    Blobel, G.5
  • 7
    • 0031586612 scopus 로고    scopus 로고
    • Multiple protein: Protein interactions between the snRNP common core proteins
    • Fury, M. G., W. Zhang, I. Christodoulopoulos, and G. W. Zieve. 1997. Multiple protein: protein interactions between the snRNP common core proteins. Exp. Cell Res. 237:63-69.
    • (1997) Exp. Cell Res. , vol.237 , pp. 63-69
    • Fury, M.G.1    Zhang, W.2    Christodoulopoulos, I.3    Zieve, G.W.4
  • 8
    • 0030474356 scopus 로고    scopus 로고
    • The highly conserved skb1 gene encodes a protein that interacts with Shk1, a fission yeast Ste20/PAK homolog
    • Gilbreth, M., P. R. Yang, D. Wang, J. Frost, A. Polverino, M. H. Cobb, and S. Marcus. 1996. The highly conserved skb1 gene encodes a protein that interacts with Shk1, a fission yeast Ste20/PAK homolog. Proc. Natl. Acad. Sci. USA 93:13802-13807.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13802-13807
    • Gilbreth, M.1    Yang, P.R.2    Wang, D.3    Frost, J.4    Polverino, A.5    Cobb, M.H.6    Marcus, S.7
  • 9
    • 0025007910 scopus 로고
    • The trimethylguanosine cap structure of U1 snRNA is a component of a bipartitie nuclear targeting signal
    • Hamm, J., S. Darzynkiewicz, M. Tahara, and I. W. Mattaj. 1990. The trimethylguanosine cap structure of U1 snRNA is a component of a bipartitie nuclear targeting signal. Cell 62:569-577.
    • (1990) Cell , vol.62 , pp. 569-577
    • Hamm, J.1    Darzynkiewicz, S.2    Tahara, M.3    Mattaj, I.W.4
  • 10
    • 0024788937 scopus 로고
    • An abundant U6 snRNP found in germ cells and embryos of Xenopus laevis
    • Hamm, J., and I. W. Mattaj. 1989. An abundant U6 snRNP found in germ cells and embryos of Xenopus laevis. EMBO J. 8:4179-4187.
    • (1989) EMBO J. , vol.8 , pp. 4179-4187
    • Hamm, J.1    Mattaj, I.W.2
  • 11
    • 0029018708 scopus 로고
    • Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system
    • Hollenberg, S. M., R. Sternglanz, P. F. Cheng, and H. Weintraub. 1995. Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system. Mol. Cell. Biol. 15:3813-3822.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3813-3822
    • Hollenberg, S.M.1    Sternglanz, R.2    Cheng, P.F.3    Weintraub, H.4
  • 12
  • 13
    • 0029891101 scopus 로고    scopus 로고
    • The structure and function of proteins involved in mammalian pre-mRNA splicing
    • Kramer, A. 1996. The structure and function of proteins involved in mammalian pre-mRNA splicing. Annu. Rev. Biochem. 65:367-409.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 367-409
    • Kramer, A.1
  • 14
    • 0032080214 scopus 로고    scopus 로고
    • pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology
    • Krapivinsky, G., W. Pu, K. Wickman, L. Krapivinsky, and D. E. Clapham. 1998. pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology. J. Biol. Chem. 273:10811-10814.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10811-10814
    • Krapivinsky, G.1    Pu, W.2    Wickman, K.3    Krapivinsky, L.4    Clapham, D.E.5
  • 15
    • 0028144541 scopus 로고
    • Molecular characterization of a swelling-induced chloride conductance regulatory protein, pICln
    • Krapivinsky, G. B., M. J. Ackerman, E. A. Gordon, L. Krapivinsky, and D. E. Clapham. 1994. Molecular characterization of a swelling-induced chloride conductance regulatory protein, pICln. Cell 76:439-448.
    • (1994) Cell , vol.76 , pp. 439-448
    • Krapivinsky, G.B.1    Ackerman, M.J.2    Gordon, E.A.3    Krapivinsky, L.4    Clapham, D.E.5
  • 17
    • 0027988478 scopus 로고
    • cDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: Evidence for a direct D1-D2 interaction
    • Lehmeier, T., V. Raker, H. Hermann, and R. Luhrmann. 1994. cDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: evidence for a direct D1-D2 interaction. Proc. Natl. Acad. Sci. USA 91:12317-12321.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12317-12321
    • Lehmeier, T.1    Raker, V.2    Hermann, H.3    Luhrmann, R.4
  • 18
    • 0025027317 scopus 로고
    • Evidence for three distinct D proteins, which react differentially with anti-Sm autoantibodies, in the cores of the major snRNPs U1, U2, U4/U6 and U5
    • Lehmeier, T., K. Foulaki, and R. Luhrmann. 1990. Evidence for three distinct D proteins, which react differentially with anti-Sm autoantibodies, in the cores of the major snRNPs U1, U2, U4/U6 and U5. Nucleic Acids Res. 18:6475-6484.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6475-6484
    • Lehmeier, T.1    Foulaki, K.2    Luhrmann, R.3
  • 19
    • 0019570066 scopus 로고
    • Monoclonal antibodies to nucleic acid-containing cellular constituents: Probes for molecular biology and autoimmune disease
    • Lerner, E. A., M. R. Lerner, J. A. Hardin, C. A. Janeway, and J. A. Steitz. 1981. Monoclonal antibodies to nucleic acid-containing cellular constituents: probes for molecular biology and autoimmune disease. Proc. Natl. Acad. Sci. USA 78:2737-2741.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2737-2741
    • Lerner, E.A.1    Lerner, M.R.2    Hardin, J.A.3    Janeway, C.A.4    Steitz, J.A.5
  • 20
    • 0030931727 scopus 로고    scopus 로고
    • The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins
    • Liu, Q., U. Fischer, F. Wang, and G. Dreyfuss. 1997. The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins. Cell 90:1013-1021.
    • (1997) Cell , vol.90 , pp. 1013-1021
    • Liu, Q.1    Fischer, U.2    Wang, F.3    Dreyfuss, G.4
  • 21
    • 0025173604 scopus 로고
    • Structure of snRNPs and their role in pre-mRNA splicing
    • Lührmann, R., B. Kastner, and M. Bach. 1990. Structure of snRNPs and their role in pre-mRNA splicing. Biochim. Biophys. Acta 1087:265-292.
    • (1990) Biochim. Biophys. Acta , vol.1087 , pp. 265-292
    • Lührmann, R.1    Kastner, B.2    Bach, M.3
  • 22
    • 0023047717 scopus 로고
    • Cap trimethylation of U snRNA is cytoplasmic and dependent on U snRNP protein binding
    • Mattaj, I. 1986. Cap trimethylation of U snRNA is cytoplasmic and dependent on U snRNP protein binding. Cell 46:905-911.
    • (1986) Cell , vol.46 , pp. 905-911
    • Mattaj, I.1
  • 24
    • 0021926473 scopus 로고
    • Nuclear segregation of U2 snRNA requires binding of specific snRNP proteins
    • Mattaj, I. W., and E. M. De Robertis. 1985. Nuclear segregation of U2 snRNA requires binding of specific snRNP proteins. Cell 40:111-118.
    • (1985) Cell , vol.40 , pp. 111-118
    • Mattaj, I.W.1    De Robertis, E.M.2
  • 25
    • 0031819679 scopus 로고    scopus 로고
    • Hypotonicity stimulates translocation of ICln in neonatal rat cardiac myocytes
    • Musch, M. W., E. M. Davis-Amaral, H. H. Vandenburgh, and L. Goldstein. 1998. Hypotonicity stimulates translocation of ICln in neonatal rat cardiac myocytes. Pflugers Arch. 436:415-422.
    • (1998) Pflugers Arch. , vol.436 , pp. 415-422
    • Musch, M.W.1    Davis-Amaral, E.M.2    Vandenburgh, H.H.3    Goldstein, L.4
  • 26
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer, E. J. C. J. Schmidt, R. Nambudripad, and T. F. Smith. 1994. The ancient regulatory-protein family of WD-repeat proteins. Nature 371:297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 27
    • 0025282484 scopus 로고
    • Nucleocytoplasmic transport and processing of small nuclear RNA precursors
    • Neuman De Vegvar, H. E., and J. E. Dahlberg. 1990. Nucleocytoplasmic transport and processing of small nuclear RNA precursors. Mol. Cell. Biol. 10:3365-3375.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3365-3375
    • Neuman De Vegvar, H.E.1    Dahlberg, J.E.2
  • 28
    • 0028903466 scopus 로고
    • Cloning of a swelling-induced chloride current related protein from rabbit heart
    • Okada, H., K. Ishii, K. Nunoki, and N. Taira. 1995. Cloning of a swelling-induced chloride current related protein from rabbit heart. Biochim. Biophys. Acta 1234:145-148.
    • (1995) Biochim. Biophys. Acta , vol.1234 , pp. 145-148
    • Okada, H.1    Ishii, K.2    Nunoki, K.3    Taira, N.4
  • 29
    • 0030775693 scopus 로고    scopus 로고
    • Nuclear import of U snRNPs requires importin β
    • Palacios, I., M. Hetzer, S. A. Adam, and I. W. Mattaj. 1997. Nuclear import of U snRNPs requires importin β. EMBO J. 16:6783-6792.
    • (1997) EMBO J. , vol.16 , pp. 6783-6792
    • Palacios, I.1    Hetzer, M.2    Adam, S.A.3    Mattaj, I.W.4
  • 30
    • 0000003605 scopus 로고
    • Isolation of the α subunits of GTP-binding regulatory proteins by affinity chromatography with immobilized βγ subunits
    • Pang, I.-H., and P. C. Sternwels. 1989. Isolation of the α subunits of GTP-binding regulatory proteins by affinity chromatography with immobilized βγ subunits. Biochemistry 86:7814-7818.
    • (1989) Biochemistry , vol.86 , pp. 7814-7818
    • Pang, I.-H.1    Sternwels, P.C.2
  • 31
    • 0026545643 scopus 로고
    • New mammalian chloride channel identified by expression cloning
    • Paulmichl, M., Y. Li, K. Wickman, E. Peralta, and D. Clapham. 1992. New mammalian chloride channel identified by expression cloning. Nature 356: 238-241.
    • (1992) Nature , vol.356 , pp. 238-241
    • Paulmichl, M.1    Li, Y.2    Wickman, K.3    Peralta, E.4    Clapham, D.5
  • 32
    • 0032567036 scopus 로고    scopus 로고
    • A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA splicing
    • Pellizzoni, L., N. Kataoka, B. Charroux, and G. Dreyfuss. 1998. A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA splicing. Cell 95:615-624.
    • (1998) Cell , vol.95 , pp. 615-624
    • Pellizzoni, L.1    Kataoka, N.2    Charroux, B.3    Dreyfuss, G.4
  • 33
    • 0030007060 scopus 로고    scopus 로고
    • The snRNP core assembly pathway: Identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro
    • Raker, V. A., G. Plessel, and R. Luhrmann. 1996. The snRNP core assembly pathway: identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro. EMBO J. 15:2256-2269.
    • (1996) EMBO J. , vol.15 , pp. 2256-2269
    • Raker, V.A.1    Plessel, G.2    Luhrmann, R.3
  • 34
    • 0024827307 scopus 로고
    • Cloned human snRNP proteins B and B′ differ only in the carboxy-terminal part
    • Van Dam, A., L Winkel, J. Zijlstra-Baalbergen, R. Smeenk, and H. T. Cuypers. 1989. Cloned human snRNP proteins B and B′ differ only in the carboxy-terminal part. EMBO J. 8:3853-3860.
    • (1989) EMBO J. , vol.8 , pp. 3853-3860
    • Van Dam, A.1    Winkel, L.2    Zijlstra-Baalbergen, J.3    Smeenk, R.4    Cuypers, H.T.5
  • 36
    • 0020560218 scopus 로고
    • Nucleocytoplasmic distribution of snRNPs and stockpiled snRNA-binding proteins during oogenesis and early development in Xenopus laevis
    • Zeller, R., T. Nyffenegger, and E. M. DeRobertis. 1983. Nucleocytoplasmic distribution of snRNPs and stockpiled snRNA-binding proteins during oogenesis and early development in Xenopus laevis. Cell 32:425-434.
    • (1983) Cell , vol.32 , pp. 425-434
    • Zeller, R.1    Nyffenegger, T.2    DeRobertis, E.M.3


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