메뉴 건너뛰기




Volumn 9, Issue 9, 2010, Pages 4554-4564

Acetylation of RNA processing proteins and cell cycle proteins in mitosis

Author keywords

acetylation; cell cycle; histone deacetylase inhibitor; mitosis; RNA processing

Indexed keywords

ANILLIN; CELL CYCLE PROTEIN; CHAPERONE; HISTONE DEACETYLASE; LYSINE; MEMBRANE PROTEIN; PROTEIN APC1; PROTEIN ELF4G; PROTEIN NUDC; RNA HELICASE; TRICHOSTATIN A; UNCLASSIFIED DRUG;

EID: 77956315751     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr100281h     Document Type: Article
Times cited : (31)

References (53)
  • 3
    • 70349974263 scopus 로고    scopus 로고
    • Quantitative analysis of the human spindle phosphoproteome at distinct mitotic stages
    • Malik, R.; Lenobel, R.; Santamaria, A.; Ries, A.; Nigg, E. A.; Korner, R. Quantitative analysis of the human spindle phosphoproteome at distinct mitotic stages J. Proteome Res. 2009, 10, 4553-4563
    • (2009) J. Proteome Res. , vol.10 , pp. 4553-4563
    • Malik, R.1    Lenobel, R.2    Santamaria, A.3    Ries, A.4    Nigg, E.A.5    Korner, R.6
  • 4
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: Codified crosstalk with other posttranslational modification
    • Yang, X.-J.; Seto, E. Lysine acetylation: codified crosstalk with other posttranslational modification Mol. Cell 2008, 31, 449-461
    • (2008) Mol. Cell , vol.31 , pp. 449-461
    • Yang, X.-J.1    Seto, E.2
  • 5
    • 62449196769 scopus 로고    scopus 로고
    • Large scale detection of ubiquitination substrates using cell extracts and protein microarrays
    • Merbl, Y.; Kirschner, M. W. Large scale detection of ubiquitination substrates using cell extracts and protein microarrays Proc. Natl. Acad. Sci. U.S.A. 2008, 106, 2543-2548
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 2543-2548
    • Merbl, Y.1    Kirschner, M.W.2
  • 6
    • 63549129144 scopus 로고    scopus 로고
    • SUMOylation and de-SUMOylation: Wrestling with life's processes
    • Yeh, E. T. H. SUMOylation and de-SUMOylation: wrestling with life's processes J. Biol. Chem. 2009, 248, 8223-8227
    • (2009) J. Biol. Chem. , vol.248 , pp. 8223-8227
    • Yeh, E.T.H.1
  • 7
    • 41949132208 scopus 로고    scopus 로고
    • Histone deacetylase 3 localizes to the mitotic spindle and is required for kinetochore-microtubule attachment
    • Ishii, S.; Kurasawa, Y.; Wong, J.; Yu-Lee, L. Histone deacetylase 3 localizes to the mitotic spindle and is required for kinetochore-microtubule attachment Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 4179-4184
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 4179-4184
    • Ishii, S.1    Kurasawa, Y.2    Wong, J.3    Yu-Lee, L.4
  • 8
    • 65949103641 scopus 로고    scopus 로고
    • SELD-TOF as a method for biomarker discovery in the urine of aristolochic-acid-treated mice
    • Huang, F.; Clifton, J.; Yang, X.; Rosenquist, T.; Hixon, D. C.; Kovacs, S.; Josic, D. SELD-TOF as a method for biomarker discovery in the urine of aristolochic-acid-treated mice Electrophoresis 2009, 30, 1168-1174
    • (2009) Electrophoresis , vol.30 , pp. 1168-1174
    • Huang, F.1    Clifton, J.2    Yang, X.3    Rosenquist, T.4    Hixon, D.C.5    Kovacs, S.6    Josic, D.7
  • 9
    • 70649093099 scopus 로고    scopus 로고
    • Proteomic characterization of plasma-derived clotting factor VIII-von Willebrand factor concentrates
    • Clifton, J. G.; Huang, F.; Kovac, S.; Yang, X.; Hixson, D. C.; Josic, D. Proteomic characterization of plasma-derived clotting factor VIII-von Willebrand factor concentrates Electrophoresis 2009, 30, 3636-3646
    • (2009) Electrophoresis , vol.30 , pp. 3636-3646
    • Clifton, J.G.1    Huang, F.2    Kovac, S.3    Yang, X.4    Hixson, D.C.5    Josic, D.6
  • 10
    • 33745972064 scopus 로고    scopus 로고
    • NudC is required for Plk1 targeting to the kinetochore and chromosome congression
    • Nishino, M.; Kurasawa, Y.; Evans, R.; Lin, S.-H.; Brinkley, B. R.; Yu-Lee, L. NudC is required for Plk1 targeting to the kinetochore and chromosome congression Curr. Biol. 2006, 16, 1414-1421
    • (2006) Curr. Biol. , vol.16 , pp. 1414-1421
    • Nishino, M.1    Kurasawa, Y.2    Evans, R.3    Lin, S.-H.4    Brinkley, B.R.5    Yu-Lee, L.6
  • 11
    • 21444446061 scopus 로고    scopus 로고
    • Translation of eukaryotic translation initiation factor 4G1 (eIF4G1) proceeds from multiple mRNAs containing a novel cap-dependent internal ribosome entry site (IRES) that is active during poliovirus infection
    • Byrd, M. P.; Zamora, M.; Lloyd, R. E. Translation of eukaryotic translation initiation factor 4G1 (eIF4G1) proceeds from multiple mRNAs containing a novel cap-dependent internal ribosome entry site (IRES) that is active during poliovirus infection J. Biol. Chem. 2005, 19, 18610-18622
    • (2005) J. Biol. Chem. , vol.19 , pp. 18610-18622
    • Byrd, M.P.1    Zamora, M.2    Lloyd, R.E.3
  • 13
    • 0023205561 scopus 로고
    • A pragmatic approach to the analysis of DNA histograms with a definable G1 peak
    • Watson, J. V.; Chambers, S. H.; Smith, P. J. A pragmatic approach to the analysis of DNA histograms with a definable G1 peak Cytometry 1987, 8, 1-8
    • (1987) Cytometry , vol.8 , pp. 1-8
    • Watson, J.V.1    Chambers, S.H.2    Smith, P.J.3
  • 14
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. Chromatin modifications and their function Cell 2007, 128, 693-705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 15
    • 42049083539 scopus 로고    scopus 로고
    • Regulation of mRNA translation during cellular division
    • Sivan, G.; Elroy-Stein, O. Regulation of mRNA translation during cellular division Cell Cycle 2008, 7, 741-744
    • (2008) Cell Cycle , vol.7 , pp. 741-744
    • Sivan, G.1    Elroy-Stein, O.2
  • 16
    • 1542344429 scopus 로고    scopus 로고
    • DEAD-box proteins: The driving forces behind RNA metabolism
    • Rocak, S.; Linder, P. DEAD-box proteins: the driving forces behind RNA metabolism Nat. Rev. Mol. Cell Biol. 2004, 5, 232-241
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 232-241
    • Rocak, S.1    Linder, P.2
  • 17
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin, O.; Banroques, J.; Tanner, N. K.; Linder, P. The DEAD-box protein family of RNA helicases Gene 2006, 367, 17-37
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 18
    • 0035834922 scopus 로고    scopus 로고
    • Characterization of the human APC1, the largest subunit of the anaphase promoting complex
    • Jorgensen, P. M.; Graslund, S.; Betz, R.; Stahl, S.; Larson, C.; Hoog, C. Characterization of the human APC1, the largest subunit of the anaphase promoting complex Gene 2001, 262, 51-59
    • (2001) Gene , vol.262 , pp. 51-59
    • Jorgensen, P.M.1    Graslund, S.2    Betz, R.3    Stahl, S.4    Larson, C.5    Hoog, C.6
  • 19
    • 45249085052 scopus 로고    scopus 로고
    • Control of mitotic exit and cytokinesis by the APC/C
    • Lindon, C. Control of mitotic exit and cytokinesis by the APC/C Biochem. Soc. Trans. 2008, 36, 405-410
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 405-410
    • Lindon, C.1
  • 20
    • 62449220573 scopus 로고    scopus 로고
    • Structure of the anaphase promoting complex/cyclosome interacting with a mitotic checkpoint complex
    • Herzog, F.; Primorac, I.; Dube, P.; Lenart, P.; Sander, B.; Mechtler, K.; Stark, H.; Peters, J.-M. Structure of the anaphase promoting complex/cyclosome interacting with a mitotic checkpoint complex Science 2009, 323, 1477-1481
    • (2009) Science , vol.323 , pp. 1477-1481
    • Herzog, F.1    Primorac, I.2    Dube, P.3    Lenart, P.4    Sander, B.5    Mechtler, K.6    Stark, H.7    Peters, J.-M.8
  • 21
    • 25844499804 scopus 로고    scopus 로고
    • Anillin is a substrate of anaphase-promoting complex/cyclosome (APC/C) that controls spatial contractility of myosin during late cytokinesis
    • Zhao, W.-M.; Fang, G. Anillin is a substrate of anaphase-promoting complex/cyclosome (APC/C) that controls spatial contractility of myosin during late cytokinesis J. Biol. Chem. 2005, 280, 33516-33524
    • (2005) J. Biol. Chem. , vol.280 , pp. 33516-33524
    • Zhao, W.-M.1    Fang, G.2
  • 22
    • 45249092172 scopus 로고    scopus 로고
    • Anillin: A pivotal organizer of the cytokinetic machinery
    • Hickson, G. R. X.; O'Farrell, P. H. Anillin: a pivotal organizer of the cytokinetic machinery Biochem. Soc. Trans. 2008, 36, 439-441
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 439-441
    • Hickson, G.R.X.1    O'farrell, P.H.2
  • 24
    • 0038686507 scopus 로고    scopus 로고
    • A role for Plk1 phosphorylation of NudC in cytokinesis
    • Zhou, T.; Aumais, J. P.; Liu, X.; Yu-Lee, L.; Erikson, R. L. A role for Plk1 phosphorylation of NudC in cytokinesis Dev. Cell 2003, 5, 127-138
    • (2003) Dev. Cell , vol.5 , pp. 127-138
    • Zhou, T.1    Aumais, J.P.2    Liu, X.3    Yu-Lee, L.4    Erikson, R.L.5
  • 27
    • 0026594997 scopus 로고
    • Enzymes involved in the dynamic equilibrium of core histone acetylation of Physarum polycephalum
    • Lopez-Rodas, G.; Brosch, G.; Golderer, G.; Lindner, H.; Grobner, P.; Loidl, P. Enzymes involved in the dynamic equilibrium of core histone acetylation of Physarum polycephalum FEBS Lett. 1992, 296, 82-86
    • (1992) FEBS Lett. , vol.296 , pp. 82-86
    • Lopez-Rodas, G.1    Brosch, G.2    Golderer, G.3    Lindner, H.4    Grobner, P.5    Loidl, P.6
  • 30
    • 14844361808 scopus 로고    scopus 로고
    • Multisite protein modification and intramolecular signaling
    • Yang, X.-J. Multisite protein modification and intramolecular signaling Oncogene 2005, 24, 1653-1662
    • (2005) Oncogene , vol.24 , pp. 1653-1662
    • Yang, X.-J.1
  • 31
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signaling at multiple levels
    • Spange, S.; Wagner, T.; Heinzel, T.; Kramer, O. H. Acetylation of non-histone proteins modulates cellular signaling at multiple levels Int. J. Biochem. Cell Biol. 2009, 41, 185-198
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 185-198
    • Spange, S.1    Wagner, T.2    Heinzel, T.3    Kramer, O.H.4
  • 32
    • 66049084037 scopus 로고    scopus 로고
    • Translation control from head to tail
    • Groppo, R.; Richter, J. D. Translation control from head to tail Curr. Opin. Cell Biol. 2009, 21, 444-451
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 444-451
    • Groppo, R.1    Richter, J.D.2
  • 33
    • 24944572189 scopus 로고    scopus 로고
    • EIF4G and CBP80 share a common origin and similar domain organization: Implications for the structure and function of eIF4G
    • Marintchev, A.; Wagner, G. eIF4G and CBP80 share a common origin and similar domain organization: Implications for the structure and function of eIF4G Biochemistry 2005, 44, 12265-12272
    • (2005) Biochemistry , vol.44 , pp. 12265-12272
    • Marintchev, A.1    Wagner, G.2
  • 35
    • 34748870653 scopus 로고    scopus 로고
    • Ribosomal slowdown mediates translational arrest during cellular division
    • Sivan, G.; Kedersha, N.; Elroy-Stein, O. Ribosomal slowdown mediates translational arrest during cellular division Mol. Cell. Biol. 2007, 27, 6639-6646
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6639-6646
    • Sivan, G.1    Kedersha, N.2    Elroy-Stein, O.3
  • 36
    • 0030945449 scopus 로고    scopus 로고
    • Domain structure of human nuclear DNA helicase II (RNA helicase A)
    • Zhang, S.; Grosse, F. Domain structure of human nuclear DNA helicase II (RNA helicase A) J. Biol. Chem. 1997, 272, 11487-11494
    • (1997) J. Biol. Chem. , vol.272 , pp. 11487-11494
    • Zhang, S.1    Grosse, F.2
  • 37
    • 2642684539 scopus 로고    scopus 로고
    • A subunit of the anaphase promoting complex is a centromere-associated protein in mammalian cells
    • Jorgensen, P. M.; Brundell, E.; Starborg, M.; Hoog, C. A subunit of the anaphase promoting complex is a centromere-associated protein in mammalian cells Mol. Cell. Biol. 1998, 18, 468-476
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 468-476
    • Jorgensen, P.M.1    Brundell, E.2    Starborg, M.3    Hoog, C.4
  • 38
    • 33747589184 scopus 로고    scopus 로고
    • The anaphase promoting complex/cyclosome: A machine designed to destroy
    • Peters, J.-M. The anaphase promoting complex/cyclosome: a machine designed to destroy Nat. Rev. Mol. Cell Biol. 2006, 7, 644-656
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 644-656
    • Peters, J.-M.1
  • 41
    • 66849140911 scopus 로고    scopus 로고
    • How to scaffold the contractile ring for a safe cytokinesis - Lessons from anillin-related proteins
    • D'Avino, P. P. How to scaffold the contractile ring for a safe cytokinesis - lessons from anillin-related proteins J. Cell Sci. 2009, 233, 1071-1079
    • (2009) J. Cell Sci. , vol.233 , pp. 1071-1079
    • D'avino, P.P.1
  • 44
    • 25144496594 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylases alter kinetochore assembly by disrupting pericentromeric heterochromatin
    • Robbins, A. R.; Jablonski, S. A.; Yen, T. J.; Yoda, K.; Robey, R.; Bates, S. E.; Sackett, D. L. Inhibitors of histone deacetylases alter kinetochore assembly by disrupting pericentromeric heterochromatin Cell Cycle 2005, 4, 717-726
    • (2005) Cell Cycle , vol.4 , pp. 717-726
    • Robbins, A.R.1    Jablonski, S.A.2    Yen, T.J.3    Yoda, K.4    Robey, R.5    Bates, S.E.6    Sackett, D.L.7
  • 45
    • 25144513926 scopus 로고    scopus 로고
    • Mitotic spindle checkpoint inactivation by trichostatin A defines a mechanism for increasing cancer cell killing by microtubule-disrupting agents
    • Dowling, M.; Voong, K. R.; Kim, M.; Keutmann, M. K.; Harris, E.; Kao, G. D. Mitotic spindle checkpoint inactivation by trichostatin A defines a mechanism for increasing cancer cell killing by microtubule-disrupting agents Cancer Biol. Ther. 2005, 4, 197-206
    • (2005) Cancer Biol. Ther. , vol.4 , pp. 197-206
    • Dowling, M.1    Voong, K.R.2    Kim, M.3    Keutmann, M.K.4    Harris, E.5    Kao, G.D.6
  • 46
    • 39849093997 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce mitotic slippage
    • Stevens, F. E.; Beamish, H.; Warrener, R.; Gabrielli, B. Histone deacetylase inhibitors induce mitotic slippage Oncogene 2007, 27, 1345-1354
    • (2007) Oncogene , vol.27 , pp. 1345-1354
    • Stevens, F.E.1    Beamish, H.2    Warrener, R.3    Gabrielli, B.4
  • 47
    • 34447115130 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce premature sister chromatid separation and override the mitotic spindle assembly checkpoint
    • Magnaghi-Jaulin, L.; Eot-Houllier, G.; Fulcrand, G.; Jualin, C. Histone deacetylase inhibitors induce premature sister chromatid separation and override the mitotic spindle assembly checkpoint Cancer Res. 2007, 67, 6360-6367
    • (2007) Cancer Res. , vol.67 , pp. 6360-6367
    • Magnaghi-Jaulin, L.1    Eot-Houllier, G.2    Fulcrand, G.3    Jualin, C.4
  • 48
    • 53049086094 scopus 로고    scopus 로고
    • Inhibition of protein deacetylation by TSA impairs microtubule- kinteochore attachment
    • Ma, Y.; Cai, S.; Cai, S.; Lu, Q.; Lu, X.; Jiang, Q.; Zhou, J.; Zhang, C. Inhibition of protein deacetylation by TSA impairs microtubule-kinteochore attachment Cell. Mol. Life Sci. 2008, 65, 3100-3109
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3100-3109
    • Ma, Y.1    Cai, S.2    Cai, S.3    Lu, Q.4    Lu, X.5    Jiang, Q.6    Zhou, J.7    Zhang, C.8
  • 50
    • 67651161889 scopus 로고    scopus 로고
    • BubR1 acetylation at prometaphase is required for modulating APC/C activity and timing of mitosis
    • Choi, E.; Choe, H.; Min, J.; Choi, J. Y.; Kim, J.; Lee, H. BubR1 acetylation at prometaphase is required for modulating APC/C activity and timing of mitosis EMBO J. 2009, 28, 2077-2089
    • (2009) EMBO J. , vol.28 , pp. 2077-2089
    • Choi, E.1    Choe, H.2    Min, J.3    Choi, J.Y.4    Kim, J.5    Lee, H.6
  • 53
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action
    • Xu, W. S.; Parmigiani, R. B.; Marks, P. A. Histone deacetylase inhibitors: molecular mechanisms of action Oncogene 2007, 26, 5541-5552
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.