메뉴 건너뛰기




Volumn 453, Issue 2, 2013, Pages 271-279

Minimal functional domains of paralogues hnRNP L and hnRNP LL exhibit mechanistic differences in exonic splicing repression

Author keywords

Alternative splicing; Heterogeneous nuclear ribonucleoprotein L (hnRNP L); Heterogeneous nuclear ribonucleoprotein LL (hnRNP LL); MS2 tethering; Spliceosome regulation

Indexed keywords

AMINO ACID; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN L;

EID: 84879558686     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130432     Document Type: Article
Times cited : (16)

References (21)
  • 1
    • 2942623743 scopus 로고    scopus 로고
    • hnRNP K: One protein multiple processes
    • DOI 10.1002/bies.20048
    • Bomsztyk, K., Denisenko, O. and Ostrowski, J. (2004) hnRNP K: one protein multiple processes. BioEssays 26, 629-638 (Pubitemid 38758340)
    • (2004) BioEssays , vol.26 , Issue.6 , pp. 629-638
    • Bomsztyk, K.1    Denisenko, O.2    Ostrowski, J.3
  • 2
    • 0036223676 scopus 로고    scopus 로고
    • The poly(C)-binding proteins: A multiplicity of functions and a search for mechanisms
    • DOI 10.1017/S1355838202024627
    • Makeyev, A. V. and Liebhaber, S. A. (2002) The poly(C)-binding proteins: a multiplicity of functions and a search for mechanisms. RNA 8, 265-278 (Pubitemid 34311177)
    • (2002) RNA , vol.8 , Issue.3 , pp. 265-278
    • Makeyev, A.V.1    Liebhaber, S.A.2
  • 4
    • 38349138834 scopus 로고    scopus 로고
    • Regulation of alternative splicing: More than just the ABCs
    • House, A. E. and Lynch, K. W. (2008) Regulation of alternative splicing: more than just the ABCs. J. Biol. Chem. 283, 1217-1221
    • (2008) J. Biol. Chem. , vol.283 , pp. 1217-1221
    • House, A.E.1    Lynch, K.W.2
  • 5
    • 0033800453 scopus 로고    scopus 로고
    • Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein
    • Markovtsov, V., Nikolic, J. M., Goldman, J. A., Turck, C. W., Chou, M. Y. and Black, D. L. (2000) Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein. Mol. Cell. Biol. 20, 7463-7479
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7463-7479
    • Markovtsov, V.1    Nikolic, J.M.2    Goldman, J.A.3    Turck, C.W.4    Chou, M.Y.5    Black, D.L.6
  • 6
    • 84864020005 scopus 로고    scopus 로고
    • Ptbp2 represses adult-specific splicing to regulate the generation of neuronal precursors in the embryonic brain
    • Licatalosi, D. D., Yano, M., Fak, J. J., Mele, A., Grabinski, S. E., Zhang, C. and Darnell, R. B. (2012) Ptbp2 represses adult-specific splicing to regulate the generation of neuronal precursors in the embryonic brain. Genes Dev. 26, 1626-1642
    • (2012) Genes Dev. , vol.26 , pp. 1626-1642
    • Licatalosi, D.D.1    Yano, M.2    Fak, J.J.3    Mele, A.4    Grabinski, S.E.5    Zhang, C.6    Darnell, R.B.7
  • 7
    • 52949090808 scopus 로고    scopus 로고
    • A cell-based screen for splicing regulators identifies hnRNP LL as a distinct signal-induced repressor of CD45 variable exon 4
    • Topp, J. D., Jackson, J., Melton, A. A. and Lynch, K. W. (2008) A cell-based screen for splicing regulators identifies hnRNP LL as a distinct signal-induced repressor of CD45 variable exon 4. RNA 14, 2038-2049
    • (2008) RNA , vol.14 , pp. 2038-2049
    • Topp, J.D.1    Jackson, J.2    Melton, A.A.3    Lynch, K.W.4
  • 8
    • 48749100692 scopus 로고    scopus 로고
    • Regulation of CD45 alternative splicing by heterogeneous ribonucleoprotein, hnRNPLL
    • Oberdoerffer, S., Moita, L. F., Neems, D., Freitas, R. P., Hacohen, N. and Rao, A. (2008) Regulation of CD45 alternative splicing by heterogeneous ribonucleoprotein, hnRNPLL. Science 321, 686-691
    • (2008) Science , vol.321 , pp. 686-691
    • Oberdoerffer, S.1    Moita, L.F.2    Neems, D.3    Freitas, R.P.4    Hacohen, N.5    Rao, A.6
  • 11
    • 84876820281 scopus 로고    scopus 로고
    • hnRNP L and hnRNP A1 induce extended U1 snRNA interactions with an exon to repress spliceosome assembly
    • Chiou, N. T., Shankarling, G. and Lynch, K. W. (2013) hnRNP L and hnRNP A1 induce extended U1 snRNA interactions with an exon to repress spliceosome assembly. Mol. Cell 49, 972-982
    • (2013) Mol. Cell , vol.49 , pp. 972-982
    • Chiou, N.T.1    Shankarling, G.2    Lynch, K.W.3
  • 12
    • 0021113926 scopus 로고
    • Interaction of R17 coat protein with synthetic variants of its ribonucleic acid binding site
    • Carey, J., Lowary, P. T. and Uhlenbeck, O. C. (1983) Interaction of R17 coat protein with synthetic variants of its ribonucleic acid binding site. Biochemistry 22, 4723-4730
    • (1983) Biochemistry , vol.22 , pp. 4723-4730
    • Carey, J.1    Lowary, P.T.2    Uhlenbeck, O.C.3
  • 13
    • 38949107432 scopus 로고    scopus 로고
    • Tethering of proteins to RNAs by bacteriophage proteins
    • DOI 10.1042/BC20070067
    • Keryer-Bibens, C., Barreau, C. and Osborne, H. B. (2008) Tethering of proteins to RNAs by bacteriophage proteins. Biol. Cell 100, 125-138 (Pubitemid 351266769)
    • (2008) Biology of the Cell , vol.100 , Issue.2 , pp. 125-138
    • Keryer-Bibens, C.1    Barreau, C.2    Osborne, H.B.3
  • 14
    • 74749089043 scopus 로고    scopus 로고
    • Context-dependent regulatory mechanism of the splicing factor hnRNP L
    • Motta-Mena, L. B., Heyd, F. and Lynch, K. W. (2010) Context-dependent regulatory mechanism of the splicing factor hnRNP L. Mol. Cell 29, 223-234
    • (2010) Mol. Cell , vol.29 , pp. 223-234
    • Motta-Mena, L.B.1    Heyd, F.2    Lynch, K.W.3
  • 15
    • 79957586580 scopus 로고    scopus 로고
    • A disease-associated polymorphism alters splicing of the human CD45 phosphatase gene by disrupting combinatorial repression by heterogeneous nuclear ribonucleoproteins (hnRNPs)
    • Motta-Mena, L. B., Smith, S. A., Mallory, M. J., Jackson, J., Wang, J. and Lynch, K. W. (2011) A disease-associated polymorphism alters splicing of the human CD45 phosphatase gene by disrupting combinatorial repression by heterogeneous nuclear ribonucleoproteins (hnRNPs). J. Biol. Chem. 286, 20043-20053
    • (2011) J. Biol. Chem. , vol.286 , pp. 20043-20053
    • Motta-Mena, L.B.1    Smith, S.A.2    Mallory, M.J.3    Jackson, J.4    Wang, J.5    Lynch, K.W.6
  • 16
    • 84862950521 scopus 로고    scopus 로고
    • Mechanisms of activation and repression by the alternative splicing factors RBFOX1/2
    • Sun, S., Zhang, Z., Fregoso, O. and Krainer, A. R. (2012) Mechanisms of activation and repression by the alternative splicing factors RBFOX1/2. RNA 18, 274-283
    • (2012) RNA , vol.18 , pp. 274-283
    • Sun, S.1    Zhang, Z.2    Fregoso, O.3    Krainer, A.R.4
  • 17
    • 0028061367 scopus 로고
    • Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins
    • Mayeda, A., Munroe, S. H., Caceres, J. F. and Krainer, A. R. (1994) Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins. EMBO J. 13, 5483-5495 (Pubitemid 24351827)
    • (1994) EMBO Journal , vol.13 , Issue.22 , pp. 5483-5495
    • Mayeda, A.1    Munroe, S.H.2    Caceres, J.F.3    Krainer, A.R.4
  • 18
    • 0032962535 scopus 로고    scopus 로고
    • hnRNP A1 recruited to an exon in vivo can function as an exon splicing silencer
    • Del Gatto-Konczak, F., Olive, M., Gensel, M.-C. and Breathnack, R. (1999) hnRNP A1 recruited to an exon in vivo can function as an exon splicing silencer. Mol. Cell. Biol. 19, 251-260 (Pubitemid 29018427)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.1 , pp. 251-260
    • Del, F.1    Olive, M.2    Gesnel, M.-C.3    Breathnach, R.4
  • 19
    • 33644861782 scopus 로고    scopus 로고
    • A splicing repressor domain in polypyrimidine tract-binding protein
    • Robinson, F. and Smith, C. W. (2006) A splicing repressor domain in polypyrimidine tract-binding protein. J. Biol. Chem. 281, 800-806
    • (2006) J. Biol. Chem. , vol.281 , pp. 800-806
    • Robinson, F.1    Smith, C.W.2
  • 21
    • 79951996054 scopus 로고    scopus 로고
    • U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression
    • Sharma, S., Maris, C., Allain, F. H. and Black, D. L. (2011) U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression. Mol. Cell 41, 579-588
    • (2011) Mol. Cell , vol.41 , pp. 579-588
    • Sharma, S.1    Maris, C.2    Allain, F.H.3    Black, D.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.