메뉴 건너뛰기




Volumn 582, Issue 2, 2008, Pages 372-378

Erratum to "PKC zeta controls DNA topoisomerase-dependent human caspase-2 pre-mRNA splicing" [FEBS Lett. 582 (2008) 372-378] (DOI:10.1016/j.febslet.2007.12.032);PKC zeta controls DNA topoisomerase-dependent human caspase-2 pre-mRNA splicing

Author keywords

Caspase 2; Cell cycle; mRNA splicing; PKC zeta; Topoisomerase

Indexed keywords

CASPASE 2; DNA TOPOISOMERASE; DNA TOPOISOMERASE INHIBITOR; PROTEIN KINASE C ZETA;

EID: 38049086171     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.01.012     Document Type: Erratum
Times cited : (9)

References (44)
  • 1
    • 0036534129 scopus 로고    scopus 로고
    • Alternative splicing: multiple control mechanisms and involvement in human disease
    • Caceres J.F., and Kornblihtt A.R. Alternative splicing: multiple control mechanisms and involvement in human disease. Trends Genet. 18 (2002) 186-193
    • (2002) Trends Genet. , vol.18 , pp. 186-193
    • Caceres, J.F.1    Kornblihtt, A.R.2
  • 2
    • 0036337915 scopus 로고    scopus 로고
    • Genomic view of alternative splicing
    • Modrek B., and Lee C. Genomic view of alternative splicing. Nat. Genet. 30 (2002) 13-19
    • (2002) Nat. Genet. , vol.30 , pp. 13-19
    • Modrek, B.1    Lee, C.2
  • 3
    • 0029046727 scopus 로고
    • Identification of heterogenous ribonucleoprotein A1 as a novel substrate for protein kinase C zeta
    • Municio M.M., Lozano J., Sanchez P., Moscat J., and Diaz-Meco M.T. Identification of heterogenous ribonucleoprotein A1 as a novel substrate for protein kinase C zeta. J. Biol. Chem. 270 (1995) 15884-15891
    • (1995) J. Biol. Chem. , vol.270 , pp. 15884-15891
    • Municio, M.M.1    Lozano, J.2    Sanchez, P.3    Moscat, J.4    Diaz-Meco, M.T.5
  • 4
    • 25844491145 scopus 로고    scopus 로고
    • Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2
    • Ngo J.C., Chakrabarti S., Ding J.H., Velasquez-Dones A., Nolen B., Aubol B.E., Aadams J.A., Fu X.D., and Ghosh G. Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2. Mol. Cell 20 (2005) 77-89
    • (2005) Mol. Cell , vol.20 , pp. 77-89
    • Ngo, J.C.1    Chakrabarti, S.2    Ding, J.H.3    Velasquez-Dones, A.4    Nolen, B.5    Aubol, B.E.6    Aadams, J.A.7    Fu, X.D.8    Ghosh, G.9
  • 5
    • 0035884180 scopus 로고    scopus 로고
    • Specific inhibition of serine- and arginine-rich splicing factors phosphorylation, spliceosome assembly, and splicing by the antitumor drug NB-506
    • Pilch B., Allemand E., Facompre M., Bailly C., Riou J.F., Soret J., and Tazi J. Specific inhibition of serine- and arginine-rich splicing factors phosphorylation, spliceosome assembly, and splicing by the antitumor drug NB-506. Cancer Res. 61 (2001) 6876-6884
    • (2001) Cancer Res. , vol.61 , pp. 6876-6884
    • Pilch, B.1    Allemand, E.2    Facompre, M.3    Bailly, C.4    Riou, J.F.5    Soret, J.6    Tazi, J.7
  • 6
    • 0033564196 scopus 로고    scopus 로고
    • Developmental regulation of SR protein phosphorylation and activity
    • Sanford J.R., and Bruzik J.P. Developmental regulation of SR protein phosphorylation and activity. Gene Dev. 13 (1999) 1513-1518
    • (1999) Gene Dev. , vol.13 , pp. 1513-1518
    • Sanford, J.R.1    Bruzik, J.P.2
  • 7
    • 0032914182 scopus 로고    scopus 로고
    • Alternative splicing and programmed cell death
    • Jiang Z.H., and Wu J.Y. Alternative splicing and programmed cell death. Proc. Soc. Exp. Biol. Med. 220 (1999) 64-72
    • (1999) Proc. Soc. Exp. Biol. Med. , vol.220 , pp. 64-72
    • Jiang, Z.H.1    Wu, J.Y.2
  • 8
    • 0028168593 scopus 로고
    • Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death
    • Wang L., Miura M., Bergeron L., Zhu H., and Yuan J. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell 78 (1994) 739-750
    • (1994) Cell , vol.78 , pp. 739-750
    • Wang, L.1    Miura, M.2    Bergeron, L.3    Zhu, H.4    Yuan, J.5
  • 9
    • 0035843138 scopus 로고    scopus 로고
    • Modulation of apoptosis by procaspase-2 short isoform: selective inhibition of chromatin condensation, apoptotic body formation and phosphatidylserine externalization
    • Droin N., Rebe C., Bichat F., Hammann A., Bertrand R., and Solary E. Modulation of apoptosis by procaspase-2 short isoform: selective inhibition of chromatin condensation, apoptotic body formation and phosphatidylserine externalization. Oncogene 20 (2001) 260-269
    • (2001) Oncogene , vol.20 , pp. 260-269
    • Droin, N.1    Rebe, C.2    Bichat, F.3    Hammann, A.4    Bertrand, R.5    Solary, E.6
  • 10
    • 0037434720 scopus 로고    scopus 로고
    • The human caspase-2 gene: alternative promoters, pre-mRNA splicing and AUG usage direct isoform-specific expression
    • Logette E., Wotawa A., Solier S., Desoche L., Solary E., and Corcos L. The human caspase-2 gene: alternative promoters, pre-mRNA splicing and AUG usage direct isoform-specific expression. Oncogene 22 (2003) 935-946
    • (2003) Oncogene , vol.22 , pp. 935-946
    • Logette, E.1    Wotawa, A.2    Solier, S.3    Desoche, L.4    Solary, E.5    Corcos, L.6
  • 11
    • 20044382311 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay among human caspases: the caspase-2S putative protein is encoded by an extremely short-lived mRNA
    • Solier S., Logette E., Desoche L., Solary E., and Corcos L. Nonsense-mediated mRNA decay among human caspases: the caspase-2S putative protein is encoded by an extremely short-lived mRNA. Cell Death Differ. 12 (2005) 687-689
    • (2005) Cell Death Differ. , vol.12 , pp. 687-689
    • Solier, S.1    Logette, E.2    Desoche, L.3    Solary, E.4    Corcos, L.5
  • 13
    • 0037191508 scopus 로고    scopus 로고
    • Differential influence of etoposide on two caspase-2 mRNA isoforms in leukemic cells
    • Wotawa A., Solier S., Logette E., Solary E., and Corcos L. Differential influence of etoposide on two caspase-2 mRNA isoforms in leukemic cells. Cancer Lett. 185 (2002) 181-189
    • (2002) Cancer Lett. , vol.185 , pp. 181-189
    • Wotawa, A.1    Solier, S.2    Logette, E.3    Solary, E.4    Corcos, L.5
  • 14
    • 4644231784 scopus 로고    scopus 로고
    • The toposome: a new twist on topoisomerase II alpha
    • Borowiec J.A. The toposome: a new twist on topoisomerase II alpha. Cell Cycle 3 (2004) 627-628
    • (2004) Cell Cycle , vol.3 , pp. 627-628
    • Borowiec, J.A.1
  • 15
    • 4143085545 scopus 로고    scopus 로고
    • Identification of toposome, a novel multisubunit complex containing topoisomerase II alpha
    • Lee C.G., Hague L.K., Li H., and Donnelly R. Identification of toposome, a novel multisubunit complex containing topoisomerase II alpha. Cell Cycle 3 (2004) 638-647
    • (2004) Cell Cycle , vol.3 , pp. 638-647
    • Lee, C.G.1    Hague, L.K.2    Li, H.3    Donnelly, R.4
  • 16
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C superfamily
    • Mellor H., and Parker P.J. The extended protein kinase C superfamily. Biochem. J. 332 Pt 2 (1998) 281-292
    • (1998) Biochem. J. , vol.332 , Issue.PART 2 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 17
    • 0035943401 scopus 로고    scopus 로고
    • Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKC zeta
    • Etienne-Manneville S., and Hall A. Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKC zeta. Cell 106 (2001) 489-498
    • (2001) Cell , vol.106 , pp. 489-498
    • Etienne-Manneville, S.1    Hall, A.2
  • 18
    • 27844539756 scopus 로고    scopus 로고
    • Protein kinase C and the regulation of the actin cytoskeleton
    • Larsson C. Protein kinase C and the regulation of the actin cytoskeleton. Cell Signal. 18 (2006) 276-284
    • (2006) Cell Signal. , vol.18 , pp. 276-284
    • Larsson, C.1
  • 20
    • 0028986193 scopus 로고
    • NF-kappa B: a lesson in family values
    • Thanos D., and Maniatis T. NF-kappa B: a lesson in family values. Cell 80 (1995) 529-532
    • (1995) Cell , vol.80 , pp. 529-532
    • Thanos, D.1    Maniatis, T.2
  • 21
    • 4444294047 scopus 로고    scopus 로고
    • The M-CSF receptor substrate and interacting protein FMIP is governed in its subcellular localization by protein kinase C-mediated phosphorylation, and thereby potentiates M-CSF-mediated differentiation
    • Mancini A., Koch A., Whetton A.D., and Tamura T. The M-CSF receptor substrate and interacting protein FMIP is governed in its subcellular localization by protein kinase C-mediated phosphorylation, and thereby potentiates M-CSF-mediated differentiation. Oncogene 23 (2004) 6581-6589
    • (2004) Oncogene , vol.23 , pp. 6581-6589
    • Mancini, A.1    Koch, A.2    Whetton, A.D.3    Tamura, T.4
  • 23
    • 0032965769 scopus 로고    scopus 로고
    • Involvement of p21 in the PKC-induced regulation of the G2/M cell cycle transition
    • Barboule N., Lafon C., Chadebech P., Vidal S., and Valette A. Involvement of p21 in the PKC-induced regulation of the G2/M cell cycle transition. FEBS Lett. 444 (1999) 32-37
    • (1999) FEBS Lett. , vol.444 , pp. 32-37
    • Barboule, N.1    Lafon, C.2    Chadebech, P.3    Vidal, S.4    Valette, A.5
  • 24
    • 0348231006 scopus 로고    scopus 로고
    • Protein kinase C delta is a prosurvival factor in human breast tumor cell lines
    • McCracken M.A., Miraglia L.J., McKay R.A., and Strobl J.S. Protein kinase C delta is a prosurvival factor in human breast tumor cell lines. Mol. Cancer Ther. 2 (2003) 273-281
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 273-281
    • McCracken, M.A.1    Miraglia, L.J.2    McKay, R.A.3    Strobl, J.S.4
  • 25
    • 0034194092 scopus 로고    scopus 로고
    • Identification of PKC-isoform-specific biological actions using pharmacological approaches
    • Way K.J., Chou E., and King G.L. Identification of PKC-isoform-specific biological actions using pharmacological approaches. Trends Pharmacol. Sci. 21 (2000) 181-187
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 181-187
    • Way, K.J.1    Chou, E.2    King, G.L.3
  • 26
    • 21644447437 scopus 로고    scopus 로고
    • Protein kinase C zeta associates with death inducing signaling complex and regulates Fas ligand-induced apoptosis
    • Leroy I., de Thonel A., Laurent G., and Quillet-Mary A. Protein kinase C zeta associates with death inducing signaling complex and regulates Fas ligand-induced apoptosis. Cell Signal. 17 (2005) 1149-1157
    • (2005) Cell Signal. , vol.17 , pp. 1149-1157
    • Leroy, I.1    de Thonel, A.2    Laurent, G.3    Quillet-Mary, A.4
  • 29
    • 0032482968 scopus 로고    scopus 로고
    • Regulation of Ich-1 pre-mRNA alternative splicing and apoptosis by mammalian splicing factors
    • Jiang Z.H., Zhang W.J., Rao Y., and Wu J.Y. Regulation of Ich-1 pre-mRNA alternative splicing and apoptosis by mammalian splicing factors. Proc. Natl. Acad. Sci. USA 95 (1998) 9155-9160
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9155-9160
    • Jiang, Z.H.1    Zhang, W.J.2    Rao, Y.3    Wu, J.Y.4
  • 31
    • 0035986359 scopus 로고    scopus 로고
    • Identification of PSF as a protein kinase Calpha-binding protein in the cell nucleus
    • Rosenberger U., Lehmann I., Weise C., Franke P., Hucho F., and Buchner K. Identification of PSF as a protein kinase Calpha-binding protein in the cell nucleus. J. Cell Biochem. 86 (2002) 394-402
    • (2002) J. Cell Biochem. , vol.86 , pp. 394-402
    • Rosenberger, U.1    Lehmann, I.2    Weise, C.3    Franke, P.4    Hucho, F.5    Buchner, K.6
  • 32
    • 0142084691 scopus 로고    scopus 로고
    • Monochloramine induces reorganization of nuclear speckles and phosphorylation of SRp30 in human colonic epithelial cells: role of protein kinase C
    • Zhu Y.Q., Lu Y., and Tan X.D. Monochloramine induces reorganization of nuclear speckles and phosphorylation of SRp30 in human colonic epithelial cells: role of protein kinase C. Am. J. Physiol. Cell Physiol. 285 (2003) C1294-C1303
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Zhu, Y.Q.1    Lu, Y.2    Tan, X.D.3
  • 33
    • 0037200032 scopus 로고    scopus 로고
    • Overexpression of the atypical protein kinase C zeta reduces topoisomerase II catalytic activity, cleavable complexes formation, and drug-induced cytotoxicity in monocytic U937 leukemia cells
    • Plo I., Hernandez H., Kohlhagen G., Lautier D., Pommier Y., and Laurent G. Overexpression of the atypical protein kinase C zeta reduces topoisomerase II catalytic activity, cleavable complexes formation, and drug-induced cytotoxicity in monocytic U937 leukemia cells. J. Biol. Chem. 277 (2002) 31407-31415
    • (2002) J. Biol. Chem. , vol.277 , pp. 31407-31415
    • Plo, I.1    Hernandez, H.2    Kohlhagen, G.3    Lautier, D.4    Pommier, Y.5    Laurent, G.6
  • 34
    • 0034005482 scopus 로고    scopus 로고
    • Differential cytotoxic pathways of topoisomerase I and II anticancer agents after overexpression of the E2F-1/DP-1 transcription factor complex
    • Hofland K., Petersen B.O., Falck J., Helin K., Jensen P.B., and Sehested M. Differential cytotoxic pathways of topoisomerase I and II anticancer agents after overexpression of the E2F-1/DP-1 transcription factor complex. Clin. Cancer Res. 6 (2000) 1488-1497
    • (2000) Clin. Cancer Res. , vol.6 , pp. 1488-1497
    • Hofland, K.1    Petersen, B.O.2    Falck, J.3    Helin, K.4    Jensen, P.B.5    Sehested, M.6
  • 36
    • 30044441988 scopus 로고    scopus 로고
    • The human SWI/SNF subunit Brm is a regulator of alternative splicing
    • Batsche E., Yaniv M., and Muchardt C. The human SWI/SNF subunit Brm is a regulator of alternative splicing. Nat. Struct. Mol. Biol. 13 (2006) 22-29
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 22-29
    • Batsche, E.1    Yaniv, M.2    Muchardt, C.3
  • 37
    • 30044440197 scopus 로고    scopus 로고
    • Chromatin, transcript elongation and alternative splicing
    • Kornblihtt A.R. Chromatin, transcript elongation and alternative splicing. Nat. Struct. Mol. Biol. 13 (2006) 5-7
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 5-7
    • Kornblihtt, A.R.1
  • 38
    • 0346732307 scopus 로고    scopus 로고
    • Influence of polymerase II processivity on alternative splicing depends on splice site strength
    • Nogues G., Munoz M.J., and Kornblihtt A.R. Influence of polymerase II processivity on alternative splicing depends on splice site strength. J. Biol. Chem. 278 (2003) 52166-52171
    • (2003) J. Biol. Chem. , vol.278 , pp. 52166-52171
    • Nogues, G.1    Munoz, M.J.2    Kornblihtt, A.R.3
  • 39
    • 33748351186 scopus 로고    scopus 로고
    • Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells
    • Listerman I., Sapra A.K., and Neugebauer K.M. Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells. Nat. Struct. Mol. Biol. 13 (2006) 815-822
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 815-822
    • Listerman, I.1    Sapra, A.K.2    Neugebauer, K.M.3
  • 42
    • 0036848091 scopus 로고    scopus 로고
    • The SR protein SRp38 represses splicing in M phase cells
    • Shin C., and Manley J.L. The SR protein SRp38 represses splicing in M phase cells. Cell 111 (2002) 407-417
    • (2002) Cell , vol.111 , pp. 407-417
    • Shin, C.1    Manley, J.L.2
  • 44
    • 33645960166 scopus 로고    scopus 로고
    • PKC zeta at the crossroad of NF-kappaB and Jak1/Stat6 signaling pathways
    • Moscat J., Rennert P., and Diaz-Meco M.T. PKC zeta at the crossroad of NF-kappaB and Jak1/Stat6 signaling pathways. Cell Death Differ. 13 (2006) 702-711
    • (2006) Cell Death Differ. , vol.13 , pp. 702-711
    • Moscat, J.1    Rennert, P.2    Diaz-Meco, M.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.