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Volumn 71, Issue 6, 2009, Pages 592-600

Microtubule interfering agents and KSP inhibitors induce the phosphorylation of the nuclear protein p54nrb, an event linked to G2/M arrest

Author keywords

2D PAGE; Nano LC ESI Q ToF; p54nrb; Paclitaxel; Phosphorylation; Vincristine

Indexed keywords

CISPLATIN; CYCLIN DEPENDENT KINASE; KINESIN; KINESIN SPINDLE PROTEIN; NUCLEAR PROTEIN; PACLITAXEL; PROTEIN INHIBITOR; PROTEIN P54 NRB; ROSCOVITINE; S TRITIL CYSTEINE; UNCLASSIFIED DRUG; VINCRISTINE SULFATE;

EID: 58249132312     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2008.09.001     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 0032006059 scopus 로고    scopus 로고
    • Microtubules and actin filaments: dynamic targets for cancer chemotherapy
    • Jordan M.A., and Wilson L. Microtubules and actin filaments: dynamic targets for cancer chemotherapy. Curr Opin Cell Biol 10 (1998) 123-130
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 123-130
    • Jordan, M.A.1    Wilson, L.2
  • 2
    • 1942438028 scopus 로고    scopus 로고
    • Microtubules as a target for anticancer drugs
    • Jordan M.A., and Wilson L. Microtubules as a target for anticancer drugs. Nat Rev Cancer 4 (2004) 253-265
    • (2004) Nat Rev Cancer , vol.4 , pp. 253-265
    • Jordan, M.A.1    Wilson, L.2
  • 3
    • 0032570594 scopus 로고    scopus 로고
    • Microtubule-interfering agents activate c-Jun N-terminal kinase/stress-activated protein kinase through both Ras and apoptosis signal-regulating kinase pathways
    • Wang T.H., Wang H.S., Ichijo H., Giannakakou P., Foster J.S., Fojo T., et al. Microtubule-interfering agents activate c-Jun N-terminal kinase/stress-activated protein kinase through both Ras and apoptosis signal-regulating kinase pathways. J Biol Chem 273 (1998) 4928-4936
    • (1998) J Biol Chem , vol.273 , pp. 4928-4936
    • Wang, T.H.1    Wang, H.S.2    Ichijo, H.3    Giannakakou, P.4    Foster, J.S.5    Fojo, T.6
  • 4
    • 0035073292 scopus 로고    scopus 로고
    • Phosphorylation of Bcl2 and regulation of apoptosis
    • Ruvolo P.P., Deng X., and May W.S. Phosphorylation of Bcl2 and regulation of apoptosis. Leukemia 15 (2001) 515-522
    • (2001) Leukemia , vol.15 , pp. 515-522
    • Ruvolo, P.P.1    Deng, X.2    May, W.S.3
  • 5
    • 0030026934 scopus 로고    scopus 로고
    • Loss of normal p53 function confers sensitization to Taxol by increasing G2/M arrest and apoptosis
    • Wahl A.F., Donaldson K.L., Fairchild C., Lee F.Y., Foster S.A., Demers G.W., et al. Loss of normal p53 function confers sensitization to Taxol by increasing G2/M arrest and apoptosis. Nat Med 2 (1996) 72-79
    • (1996) Nat Med , vol.2 , pp. 72-79
    • Wahl, A.F.1    Donaldson, K.L.2    Fairchild, C.3    Lee, F.Y.4    Foster, S.A.5    Demers, G.W.6
  • 6
    • 33749551905 scopus 로고    scopus 로고
    • Can mutations in gamma-actin modulate the toxicity of microtubule targeting agents?
    • Fojo T. Can mutations in gamma-actin modulate the toxicity of microtubule targeting agents?. J Natl Cancer Inst 98 (2006) 1345-1347
    • (2006) J Natl Cancer Inst , vol.98 , pp. 1345-1347
    • Fojo, T.1
  • 9
    • 0030612145 scopus 로고    scopus 로고
    • Phosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150
    • Blangy A., Arnaud L., and Nigg E.A. Phosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150. J Biol Chem 272 (1997) 19418-19424
    • (1997) J Biol Chem , vol.272 , pp. 19418-19424
    • Blangy, A.1    Arnaud, L.2    Nigg, E.A.3
  • 10
    • 33846523617 scopus 로고    scopus 로고
    • Targeted anti-mitotic therapies: can we improve on tubulin agents?
    • Jackson J.R., Patrick D.R., Dar M.M., and Huang P.S. Targeted anti-mitotic therapies: can we improve on tubulin agents?. Nat Rev Cancer 7 (2007) 107-117
    • (2007) Nat Rev Cancer , vol.7 , pp. 107-117
    • Jackson, J.R.1    Patrick, D.R.2    Dar, M.M.3    Huang, P.S.4
  • 11
    • 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
  • 12
    • 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
  • 13
    • 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
  • 14
    • 0034720780 scopus 로고    scopus 로고
    • PSF/p54(nrb) stimulates "jumping" of DNA topoisomerase I between separate DNA helices
    • Straub T., Knudsen B.R., and Boege F. PSF/p54(nrb) stimulates "jumping" of DNA topoisomerase I between separate DNA helices. Biochemistry 39 (2000) 7552-7558
    • (2000) Biochemistry , vol.39 , pp. 7552-7558
    • Straub, T.1    Knudsen, B.R.2    Boege, F.3
  • 15
    • 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
  • 16
    • 29044449819 scopus 로고    scopus 로고
    • Systematic screening for genes specifically expressed in the anterior neuroectoderm during early Xenopus development
    • Takahashi N., Tochimoto N., Ohmori S.Y., Mamada H., Itoh M., Inamori M., et al. Systematic screening for genes specifically expressed in the anterior neuroectoderm during early Xenopus development. Int J Dev Biol 49 (2005) 939-951
    • (2005) Int J Dev Biol , vol.49 , pp. 939-951
    • Takahashi, N.1    Tochimoto, N.2    Ohmori, S.Y.3    Mamada, H.4    Itoh, M.5    Inamori, M.6
  • 17
    • 34247869080 scopus 로고    scopus 로고
    • Switched alternative splicing of oncogene CoAA during embryonal carcinoma stem cell differentiation
    • Yang Z., Sui Y., Xiong S., Liour S.S., Phillips A.C., and Ko L. Switched alternative splicing of oncogene CoAA during embryonal carcinoma stem cell differentiation. Nucleic Acids Res 35 (2007) 1919-1932
    • (2007) Nucleic Acids Res , vol.35 , pp. 1919-1932
    • Yang, Z.1    Sui, Y.2    Xiong, S.3    Liour, S.S.4    Phillips, A.C.5    Ko, L.6
  • 19
    • 33846940789 scopus 로고    scopus 로고
    • Vincristine regulates the phosphorylation of the antiapoptotic protein HSP27 in breast cancer cells
    • Casado P., Zuazua-Villar P., del Valle E., Martinez-Campa C., Lazo P.S., and Ramos S. Vincristine regulates the phosphorylation of the antiapoptotic protein HSP27 in breast cancer cells. Cancer Lett 247 (2007) 273-282
    • (2007) Cancer Lett , vol.247 , pp. 273-282
    • Casado, P.1    Zuazua-Villar, P.2    del Valle, E.3    Martinez-Campa, C.4    Lazo, P.S.5    Ramos, S.6
  • 20
    • 24044491542 scopus 로고    scopus 로고
    • Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cell, time-of-flight mass spectrometer: II. New developments in Protein Prospector allow for reliable and comprehensive automatic analysis of large datasets
    • Chalkley R.J., Baker P.R., Huang L., Hansen K.C., Allen N.P., Rexach M., et al. Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cell, time-of-flight mass spectrometer: II. New developments in Protein Prospector allow for reliable and comprehensive automatic analysis of large datasets. Mol Cell Proteomics 4 (2005) 1194-1204
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1194-1204
    • Chalkley, R.J.1    Baker, P.R.2    Huang, L.3    Hansen, K.C.4    Allen, N.P.5    Rexach, M.6
  • 22
    • 37149027185 scopus 로고    scopus 로고
    • Quantitative proteome analysis of cisplatin-induced apoptotic Jurkat T cells by stable isotope labeling with amino acids in cell culture, SDS-PAGE, and LC-MALDI-TOF/TOF MS
    • Schmidt F., Hustoft H.K., Strozynski M., Dimmler C., Rudel T., and Thiede B. Quantitative proteome analysis of cisplatin-induced apoptotic Jurkat T cells by stable isotope labeling with amino acids in cell culture, SDS-PAGE, and LC-MALDI-TOF/TOF MS. Electrophoresis 28 (2007) 4359-4368
    • (2007) Electrophoresis , vol.28 , pp. 4359-4368
    • Schmidt, F.1    Hustoft, H.K.2    Strozynski, M.3    Dimmler, C.4    Rudel, T.5    Thiede, B.6
  • 23
    • 0242413674 scopus 로고    scopus 로고
    • Proteome analysis of vinca alkaloid response and resistance in acute lymphoblastic leukemia reveals novel cytoskeletal alterations
    • Verrills N.M., Walsh B.J., Cobon G.S., Hains P.G., and Kavallaris M. Proteome analysis of vinca alkaloid response and resistance in acute lymphoblastic leukemia reveals novel cytoskeletal alterations. J Biol Chem 278 (2003) 45082-45093
    • (2003) J Biol Chem , vol.278 , pp. 45082-45093
    • Verrills, N.M.1    Walsh, B.J.2    Cobon, G.S.3    Hains, P.G.4    Kavallaris, M.5
  • 24
  • 25
    • 0035235736 scopus 로고    scopus 로고
    • Mitotic kinases as regulators of cell division and its checkpoints
    • Nigg E.A. Mitotic kinases as regulators of cell division and its checkpoints. Nat Rev Mol Cell Biol 2 (2001) 21-32
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 21-32
    • Nigg, E.A.1
  • 26
    • 21644480795 scopus 로고    scopus 로고
    • Cdc2-mediated inhibition of epidermal growth factor activation of the extracellular signal-regulated kinase pathway during mitosis
    • Dangi S., and Shapiro P. Cdc2-mediated inhibition of epidermal growth factor activation of the extracellular signal-regulated kinase pathway during mitosis. J Biol Chem 280 (2005) 24524-24531
    • (2005) J Biol Chem , vol.280 , pp. 24524-24531
    • Dangi, S.1    Shapiro, P.2
  • 27
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil S.A., Villen J., Gerber S.A., Rush J., and Gygi S.P. A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol 24 (2006) 1285-1292
    • (2006) Nat Biotechnol , vol.24 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 28
    • 0037844887 scopus 로고    scopus 로고
    • Mitotic regulation of ribosomal S6 kinase 1 involves Ser/Thr, Pro phosphorylation of consensus and non-consensus sites by Cdc2
    • Shah O.J., Ghosh S., and Hunter T. Mitotic regulation of ribosomal S6 kinase 1 involves Ser/Thr, Pro phosphorylation of consensus and non-consensus sites by Cdc2. J Biol Chem 278 (2003) 16433-16442
    • (2003) J Biol Chem , vol.278 , pp. 16433-16442
    • Shah, O.J.1    Ghosh, S.2    Hunter, T.3
  • 29
    • 13444259420 scopus 로고    scopus 로고
    • The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1
    • Proteau A., Blier S., Albert A.L., Lavoie S.B., Traish A.M., and Vincent M. The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1. J Mol Biol 346 (2005) 1163-1172
    • (2005) J Mol Biol , vol.346 , pp. 1163-1172
    • Proteau, A.1    Blier, S.2    Albert, A.L.3    Lavoie, S.B.4    Traish, A.M.5    Vincent, M.6
  • 30
    • 0035985177 scopus 로고    scopus 로고
    • Identification of genes periodically expressed in the human cell cycle and their expression in tumors
    • Whitfield M.L., Sherlock G., Saldanha A.J., Murray J.I., Ball C.A., Alexander K.E., et al. Identification of genes periodically expressed in the human cell cycle and their expression in tumors. Mol Biol Cell 13 (2002) 1977-2000
    • (2002) Mol Biol Cell , vol.13 , pp. 1977-2000
    • Whitfield, M.L.1    Sherlock, G.2    Saldanha, A.J.3    Murray, J.I.4    Ball, C.A.5    Alexander, K.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.