메뉴 건너뛰기




Volumn 288, Issue 12, 2013, Pages 8575-8584

HnRNP U enhances caspase-9 splicing and is modulated by AKT-dependent phosphorylation of hnRNP L

Author keywords

[No Author keywords available]

Indexed keywords

DOWN-REGULATION; PHOSPHOINOSITIDES; PRE-MRNA; SPLICE VARIANTS;

EID: 84875428613     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.443333     Document Type: Article
Times cited : (68)

References (24)
  • 1
    • 34250308322 scopus 로고    scopus 로고
    • Apoptosis: A review of programmed cell death
    • DOI 10.1080/01926230701320337, PII 779478428
    • Elmore, S. (2007) Apoptosis. A review of programmed cell death. Toxicol. Pathol. 35, 495-516 (Pubitemid 46911891)
    • (2007) Toxicologic Pathology , vol.35 , Issue.4 , pp. 495-516
    • Elmore, S.1
  • 2
    • 0033593201 scopus 로고    scopus 로고
    • A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis
    • Seol, D.-W., and Billiar, T. R. (1999) A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis. J. Biol. Chem. 274, 2072-2076
    • (1999) J. Biol. Chem. , vol.274 , pp. 2072-2076
    • Seol, D.-W.1    Billiar, T.R.2
  • 3
    • 0033104331 scopus 로고    scopus 로고
    • Identification of an endogenous dominant-negative short isoform of caspase-9 that can regulate apoptosis
    • Srinivasula, S. M., Ahmad, M., Guo, Y., Zhan, Y., Lazebnik, Y., Fernandes- Alnemri, T., and Alnemri, E. S. (1999) Identification of an endogenous dominant-negative short isoform of caspase-9 that can regulate apoptosis. Cancer Res. 59, 999-1002 (Pubitemid 29135957)
    • (1999) Cancer Research , vol.59 , Issue.5 , pp. 999-1002
    • Srinivasula, S.M.1    Ahmad, M.2    Guo, Y.3    Zhan, Y.4    Lazebnik, Y.5    Fernandes-Alnemri, T.6    Alnemri, E.S.7
  • 5
    • 78549234102 scopus 로고    scopus 로고
    • Alternative splicing of caspase-9 is modulated by the phosphoinositide 3-kinase/Akt pathway via phosphorylation of SRp30a
    • Shultz, J. C., Goehe, R. W., Wijesinghe, D. S., Murudkar, C., Hawkins, A. J., Shay, J. W., Minna, J. D., and Chalfant, C. E. (2010) Alternative splicing of caspase-9 is modulated by the phosphoinositide 3-kinase/Akt pathway via phosphorylation of SRp30a. Cancer Res. 70, 9185-9196
    • (2010) Cancer Res. , vol.70 , pp. 9185-9196
    • Shultz, J.C.1    Goehe, R.W.2    Wijesinghe, D.S.3    Murudkar, C.4    Hawkins, A.J.5    Shay, J.W.6    Minna, J.D.7    Chalfant, C.E.8
  • 6
    • 0037066727 scopus 로고    scopus 로고
    • De novo ceramide regulates the alternative splicing of caspase 9 and Bcl-x in A549 lung adenocarcinoma cells. Dependence on protein phosphatase-1
    • DOI 10.1074/jbc.M112010200
    • Chalfant, C. E., Rathman, K., Pinkerman, R. L., Wood, R. E., Obeid, L. M., Ogretmen, B., and Hannun, Y. A. (2002) De novo ceramide regulates the alternative splicing of caspase-9 and Bcl-x in A549 lung adenocarcinoma cells. Dependence on protein phosphatase-1. J. Biol. Chem. 277, 12587-12595 (Pubitemid 34952617)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 12587-12595
    • Chalfant, C.E.1    Rathman, K.2    Pinkerman, R.L.3    Wood, R.E.4    Obeid, L.M.5    Ogretmen, B.6    Hannun, Y.A.7
  • 7
    • 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 ceramideresponsiveness. 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
  • 9
    • 0026740718 scopus 로고
    • Primary structure and binding activity of the hnRNP U protein. Binding RNA through RGG box
    • Kiledjian, M., and Dreyfuss, G. (1992) Primary structure and binding activity of the hnRNP U protein. Binding RNA through RGG box. EMBO J. 11, 2655-2664
    • (1992) EMBO J. , vol.11 , pp. 2655-2664
    • Kiledjian, M.1    Dreyfuss, G.2
  • 10
    • 0028773273 scopus 로고
    • Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclearmatrix protein which binds DNA and RNA in vivo and in vitro
    • Fackelmayer, F. O., Dahm, K., Renz, A., Ramsperger, U., and Richter, A. (1994) Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclearmatrix protein which binds DNA and RNA in vivo and in vitro. Eur. J. Biochem. 221, 749-757
    • (1994) Eur. J. Biochem. , vol.221 , pp. 749-757
    • Fackelmayer, F.O.1    Dahm, K.2    Renz, A.3    Ramsperger, U.4    Richter, A.5
  • 12
    • 0032850595 scopus 로고    scopus 로고
    • hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation
    • Kim, M. K., and Nikodem, V. M. (1999) hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation. Mol. Cell Biol. 19, 6833-6844 (Pubitemid 29441867)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.10 , pp. 6833-6844
    • Kim, M.K.1    Nikodem, V.M.2
  • 14
    • 53549100755 scopus 로고    scopus 로고
    • The histone acetyltransferase PCAF associates with actin and hnRNP U for RNA polymerase II transcription
    • Obrdlik, A., Kukalev, A., Louvet, E., Farrants, A. K., Caputo, L., and Percipalle, P. (2008) The histone acetyltransferase PCAF associates with actin and hnRNP U for RNA polymerase II transcription. Mol. Cell Biol. 28, 6342-6357
    • (2008) Mol. Cell Biol. , vol.28 , pp. 6342-6357
    • Obrdlik, A.1    Kukalev, A.2    Louvet, E.3    Farrants, A.K.4    Caputo, L.5    Percipalle, P.6
  • 15
    • 33845642707 scopus 로고    scopus 로고
    • hnRNP-U enhances the expression of specific genes by stabilizing mRNA
    • DOI 10.1016/j.febslet.2006.11.062, PII S0014579306014037
    • Yugami, M., Kabe, Y., Yamaguchi, Y., Wada, T., and Handa, H. (2007) hnRNP-U enhances the expression of specific genes by stabilizing mRNA. FEBS Lett. 581, 1-7 (Pubitemid 44960272)
    • (2007) FEBS Letters , vol.581 , Issue.1 , pp. 1-7
    • Yugami, M.1    Kabe, Y.2    Yamaguchi, Y.3    Wada, T.4    Handa, H.5
  • 16
    • 77956607961 scopus 로고    scopus 로고
    • The matrix protein hnRNP U is required for chromosomal localization of Xist RNA
    • Hasegawa, Y., Brockdorff, N., Kawano, S., Tsutui, K., Tsutui, K., and Nakagawa, S. (2010) The matrix protein hnRNP U is required for chromosomal localization of Xist RNA. Dev. Cell 19, 469-476
    • (2010) Dev. Cell , vol.19 , pp. 469-476
    • Hasegawa, Y.1    Brockdorff, N.2    Kawano, S.3    Tsutui, K.4    Tsutui, K.5    Nakagawa, S.6
  • 17
    • 0347355216 scopus 로고    scopus 로고
    • Scaffold attachment factor A (SAF-A) is concentrated in inactive X chromosoe territories through its RGG domain
    • DOI 10.1007/s00412-003-0258-0
    • Helbig, R., and Fackelmayer, F. O. (2003) Scaffold attachment factor A (SAF-A) is concentrated in inactive X chromosome territories through its RGG domain. Chromosoma 112, 173-182 (Pubitemid 38063151)
    • (2003) Chromosoma , vol.112 , Issue.4 , pp. 173-182
    • Helbig, R.1    Fackelmayer, F.O.2
  • 18
    • 36749010238 scopus 로고    scopus 로고
    • Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation
    • DOI 10.1016/j.molcel.2007.09.023, PII S1097276507006351
    • Fu, D., and Collins, K. (2007) Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation. Mol. Cell 28, 773-785 (Pubitemid 350217053)
    • (2007) Molecular Cell , vol.28 , Issue.5 , pp. 773-785
    • Fu, D.1    Collins, K.2
  • 19
    • 84862807502 scopus 로고    scopus 로고
    • Nuclear matrix factor hnRNP U/SAF-A exerts a global control of alternative splicing by regulating U2 snRNP maturation
    • Xiao, R., Tang, P., Yang, B., Huang, J., Zhou, Y., Shao, C., Li, H., Sun, H., Zhang, Y., and Fu, X. D. (2012) Nuclear matrix factor hnRNP U/SAF-A exerts a global control of alternative splicing by regulating U2 snRNP maturation. Mol. Cell 45, 656-668
    • (2012) Mol. Cell , vol.45 , pp. 656-668
    • Xiao, R.1    Tang, P.2    Yang, B.3    Huang, J.4    Zhou, Y.5    Shao, C.6    Li, H.7    Sun, H.8    Zhang, Y.9    Fu, X.D.10
  • 20
    • 61849155778 scopus 로고    scopus 로고
    • HnRNP-U is a specific DNA-dependent protein kinase substrate phosphorylated in response to DNA double-strand breaks
    • Berglund, F. M., and Clarke, P. R. (2009) hnRNP-U is a specific DNA-dependent protein kinase substrate phosphorylated in response to DNA double-strand breaks. Biochem. Biophys. Res. Commun. 381, 59-64
    • (2009) Biochem. Biophys. Res. Commun. , vol.381 , pp. 59-64
    • Berglund, F.M.1    Clarke, P.R.2
  • 21
    • 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 37, 223-234
    • (2010) Mol. Cell , vol.37 , pp. 223-234
    • Motta-Mena, L.B.1    Heyd, F.2    Lynch, K.W.3
  • 22
    • 70449840425 scopus 로고    scopus 로고
    • Cell nonhomologous end joining capacity controls SAF-A phosphorylation by DNA-PK in response toDNAdouble-strand breaks inducers
    • Britton, S., Froment, C., Frit, P., Monsarrat, B., Salles, B., and Calsou, P. (2009) Cell nonhomologous end joining capacity controls SAF-A phosphorylation by DNA-PK in response toDNAdouble-strand breaks inducers. Cell Cycle 8, 3717-3722
    • (2009) Cell Cycle , vol.8 , pp. 3717-3722
    • Britton, S.1    Froment, C.2    Frit, P.3    Monsarrat, B.4    Salles, B.5    Calsou, P.6
  • 23
    • 0026515523 scopus 로고
    • Characterization and primary structure of the poly (C)-binding heterogeneous nuclear ribonucleoprotein complex K protein
    • Matunis, M. J., Michael, W. M., and Dreyfuss, G. (1992) Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein. Mol. Cell. Biol. 12, 164-171
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 164-171
    • Matunis, M.J.1    Michael, W.M.2    Dreyfuss, G.3
  • 24
    • 44249086425 scopus 로고    scopus 로고
    • Non-small cell lung cancer: Epidemiology, risk factors, treatment, and survivorship
    • DOI 10.4065/83.5.584
    • Molina, J. R., Yang, P., Cassivi, S. D., Schild, S. E., and Adjei A. (2008) Non-small cell lung cancer. Epidemiology, risk factors, treatment and survivorship. Mayo Clin. Proc. 83, 584-594 (Pubitemid 351720831)
    • (2008) Mayo Clinic Proceedings , vol.83 , Issue.5 , pp. 584-594
    • Molina, J.R.1    Yang, P.2    Cassivi, S.D.3    Schild, S.E.4    Adjei, A.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.