메뉴 건너뛰기




Volumn 52, Issue 1, 2012, Pages 135-145

Lysine post-translational modifications and the cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA; PROKARYOTA;

EID: 84867611373     PISSN: 00711365     EISSN: None     Source Type: Journal    
DOI: 10.1042/BSE0520135     Document Type: Article
Times cited : (23)

References (53)
  • 1
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T.D. and Borisy, G.G. (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453-465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 2
    • 2642579936 scopus 로고    scopus 로고
    • Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex
    • Millard, T.H., Sharp, S.J. and Machesky, L.M. (2004) Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex. Biochem. J. 380, 1-17
    • (2004) Biochem. J. , vol.380 , pp. 1-17
    • Millard, T.H.1    Sharp, S.J.2    Machesky, L.M.3
  • 3
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard, T.D. and Cooper, J.A. (2009) Actin, a central player in cell shape and movement. Science 326, 1208-1212
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 5
    • 0033791649 scopus 로고    scopus 로고
    • Structural insights into microtubule function
    • Nogales, E. (2000) Structural insights into microtubule function. Annu. Rev. Biochem. 69, 277-302
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 277-302
    • Nogales, E.1
  • 6
    • 0035141277 scopus 로고    scopus 로고
    • The tubulin fraternity: Alpha to eta
    • Dutcher, S.K. (2001) The tubulin fraternity: alpha to eta. Curr. Opin. Cell Biol. 13, 49-54
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 49-54
    • Dutcher, S.K.1
  • 8
    • 44149106941 scopus 로고    scopus 로고
    • A new role for cortactin in invadopodia: Regulation of protease secretion
    • Clark, E.S. and Weaver, A.M. (2008) A new role for cortactin in invadopodia: regulation of protease secretion. Eur. J. Cell Biol. 87, 581-590
    • (2008) Eur. J. Cell Biol. , vol.87 , pp. 581-590
    • Clark, E.S.1    Weaver, A.M.2
  • 9
    • 79953133501 scopus 로고    scopus 로고
    • HDAC3-dependent reversible lysine acetylation of cardiac myosin heavy chain isoforms modulates their enzymatic and motor activity
    • Samant, S.A., Courson, D.S., Sundaresan, N.R., Pillai, V.B., Tan, M., Zhao, Y., Shroff, S.G., Rock, R.S. and Gupta, M.P. (2011) HDAC3-dependent reversible lysine acetylation of cardiac myosin heavy chain isoforms modulates their enzymatic and motor activity. J. Biol. Chem. 286, 5567-5577
    • (2011) J. Biol. Chem. , vol.286 , pp. 5567-5577
    • Samant, S.A.1    Courson, D.S.2    Sundaresan, N.R.3    Pillai, V.B.4    Tan, M.5    Zhao, Y.6    Shroff, S.G.7    Rock, R.S.8    Gupta, M.P.9
  • 11
    • 0032559341 scopus 로고    scopus 로고
    • A structural scaffolding of intermediate filaments in health and disease
    • Fuchs, E. and Cleveland, D.W. (1998) A structural scaffolding of intermediate filaments in health and disease. Science 279, 514-519
    • (1998) Science , vol.279 , pp. 514-519
    • Fuchs, E.1    Cleveland, D.W.2
  • 14
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • Haggarty, S.J., Koeller, K.M., Wong, J.C., Grozinger, C.M. and Schreiber, S.L. (2003) Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc. Natl. Acad. Sci. U.S.A. 100, 4389-4394
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Grozinger, C.M.4    Schreiber, S.L.5
  • 17
    • 77955330151 scopus 로고    scopus 로고
    • Myc-nick: A cytoplasmic cleavage product of Myc that promotes α-tubulin acetylation and cell differentiation
    • Conacci-Sorrell, M., Ngouenet, C. and Eisenman, R.N. (2010) Myc-nick: a cytoplasmic cleavage product of Myc that promotes α-tubulin acetylation and cell differentiation. Cell 142, 480-493
    • (2010) Cell , vol.142 , pp. 480-493
    • Conacci-Sorrell, M.1    Ngouenet, C.2    Eisenman, R.N.3
  • 19
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim, S.C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L. et al. (2006) Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol. Cell 23, 607-618
    • (2006) Mol. Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3    Xu, Y.4    Ball, H.5    Pei, J.6    Cheng, T.7    Kho, Y.8    Xiao, H.9    Xiao, L.10
  • 22
    • 60849084173 scopus 로고    scopus 로고
    • Application of high-content analysis to the study of post-translational modifications of the cytoskeleton
    • Drake, P.J., Griffiths, G.J., Shaw, L., Benson, R.P. and Corfe, B.M. (2009) Application of high-content analysis to the study of post-translational modifications of the cytoskeleton. J. Proteome Res. 8, 28-34
    • (2009) J. Proteome Res. , vol.8 , pp. 28-34
    • Drake, P.J.1    Griffiths, G.J.2    Shaw, L.3    Benson, R.P.4    Corfe, B.M.5
  • 23
    • 38949146374 scopus 로고    scopus 로고
    • Proteomic analyses of intermediate filaments reveals cytokeratin 8 is highly acetylated: Implications for colorectal epithelial homeostasis
    • Leech, S.H., Evans, C.A., Shaw, L., Wong, C.H., Connolly, J., Griffiths, J.R., Whetton, A.D. and Corfe, B.M. (2008) Proteomic analyses of intermediate filaments reveals cytokeratin 8 is highly acetylated: implications for colorectal epithelial homeostasis. Proteomics 8, 279-288
    • (2008) Proteomics , vol.8 , pp. 279-288
    • Leech, S.H.1    Evans, C.A.2    Shaw, L.3    Wong, C.H.4    Connolly, J.5    Griffiths, J.R.6    Whetton, A.D.7    Corfe, B.M.8
  • 24
    • 11144224272 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus
    • Naranatt, P.P., Krishnan, H.H., Smith, M.S. and Chandran, B. (2005) Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus. J. Virol. 79, 1191-1206
    • (2005) J. Virol. , vol.79 , pp. 1191-1206
    • Naranatt, P.P.1    Krishnan, H.H.2    Smith, M.S.3    Chandran, B.4
  • 25
    • 58149291495 scopus 로고    scopus 로고
    • Rapid microtubule bundling and stabilization by the Streptococcus pneumoniae neurotoxin pneumolysin in a cholesterol-dependent, non-lytic and Src-kinase dependent manner inhibits intracellular trafficking
    • Iliev, A.I., Djannatian, J.R., Opazo, F., Gerber, J., Nau, R., Mitchell, T.J. and Wouters, F.S. (2009) Rapid microtubule bundling and stabilization by the Streptococcus pneumoniae neurotoxin pneumolysin in a cholesterol-dependent, non-lytic and Src-kinase dependent manner inhibits intracellular trafficking. Mol. Microbiol. 71, 461-477
    • (2009) Mol. Microbiol. , vol.71 , pp. 461-477
    • Iliev, A.I.1    Djannatian, J.R.2    Opazo, F.3    Gerber, J.4    Nau, R.5    Mitchell, T.J.6    Wouters, F.S.7
  • 27
    • 34948905714 scopus 로고    scopus 로고
    • P180 is involved in the interaction between the endoplasmic reticulum and microtubules through a novel microtubule-binding and bundling domain
    • Ogawa-Goto, K., Tanaka, K., Ueno, T., Kurata, T., Sata, T. and Irie, S. (2007) p180 is involved in the interaction between the endoplasmic reticulum and microtubules through a novel microtubule-binding and bundling domain. Mol. Biol. Cell 18, 3741-3751
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3741-3751
    • Ogawa-Goto, K.1    Tanaka, K.2    Ueno, T.3    Kurata, T.4    Sata, T.5    Irie, S.6
  • 28
    • 0024573607 scopus 로고
    • Establishment of a stable, acetylated microtubule bundle during neuronal commitment
    • Falconer, M.M., Vielkind, U. and Brown, D.L. (1989) Establishment of a stable, acetylated microtubule bundle during neuronal commitment. Cell Motil. Cytoskeleton 12, 169-180
    • (1989) Cell Motil. Cytoskeleton , vol.12 , pp. 169-180
    • Falconer, M.M.1    Vielkind, U.2    Brown, D.L.3
  • 30
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre, J.P., Godin, J.D., Charrin, B.C., Cordelieres, F.P., King, S.J., Humbert, S. and Saudou, F. (2007) Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci. 27, 3571-3583
    • (2007) J. Neurosci. , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelieres, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 31
    • 67749120701 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of the formin mDia2 upon completion of cell division
    • DeWard, A.D. and Alberts, A.S. (2009) Ubiquitin-mediated degradation of the formin mDia2 upon completion of cell division. J. Biol. Chem. 284, 20061-20069
    • (2009) J. Biol. Chem. , vol.284 , pp. 20061-20069
    • DeWard, A.D.1    Alberts, A.S.2
  • 32
    • 77956663124 scopus 로고    scopus 로고
    • Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation
    • Zhang, F., Saha, S., Shabalina, S.A. and Kashina, A. (2010) Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation. Science 329, 1534-1537
    • (2010) Science , vol.329 , pp. 1534-1537
    • Zhang, F.1    Saha, S.2    Shabalina, S.A.3    Kashina, A.4
  • 34
    • 79952688075 scopus 로고    scopus 로고
    • Determining nuclear shape: The role of farnesylated nuclear membrane proteins
    • Polychronidou, M. and Grosshans, J. (2011) Determining nuclear shape: the role of farnesylated nuclear membrane proteins. Nucleus 2, 17-23
    • (2011) Nucleus , vol.2 , pp. 17-23
    • Polychronidou, M.1    Grosshans, J.2
  • 35
    • 12344259997 scopus 로고    scopus 로고
    • Intranuclear membrane structure formations by CaaX-containing nuclear proteins
    • Ralle, T., Grund, C., Franke, W.W. and Stick, R. (2004) Intranuclear membrane structure formations by CaaX-containing nuclear proteins. J. Cell Sci. 117, 6095-6104
    • (2004) J. Cell Sci. , vol.117 , pp. 6095-6104
    • Ralle, T.1    Grund, C.2    Franke, W.W.3    Stick, R.4
  • 36
    • 0037104733 scopus 로고    scopus 로고
    • Protective role of phosphorylation in turnover of glial fibrillary acidic protein in mice
    • Takemura, M., Gomi, H., Colucci-Guyon, E. and Itohara, S. (2002) Protective role of phosphorylation in turnover of glial fibrillary acidic protein in mice. J. Neurosci. 22, 6972-6979
    • (2002) J. Neurosci. , vol.22 , pp. 6972-6979
    • Takemura, M.1    Gomi, H.2    Colucci-Guyon, E.3    Itohara, S.4
  • 37
    • 71549169907 scopus 로고    scopus 로고
    • SUMO regulates the assembly and function of a cytoplasmic intermediate filament protein in C. elegans
    • Kaminsky, R., Denison, C., Bening-Abu-Shach, U., Chisholm, A.D., Gygi, S.P. and Broday, L. (2009) SUMO regulates the assembly and function of a cytoplasmic intermediate filament protein in C. elegans. Dev. Cell 17, 724-735
    • (2009) Dev. Cell , vol.17 , pp. 724-735
    • Kaminsky, R.1    Denison, C.2    Bening-Abu-Shach, U.3    Chisholm, A.D.4    Gygi, S.P.5    Broday, L.6
  • 38
    • 68849106856 scopus 로고    scopus 로고
    • "IF-pathies": A broad spectrum of intermediate filament-associated diseases
    • Omary, M.B. (2009) "IF-pathies": a broad spectrum of intermediate filament-associated diseases. J. Clin. Invest. 119, 1756-1762
    • (2009) J. Clin. Invest. , vol.119 , pp. 1756-1762
    • Omary, M.B.1
  • 39
    • 0017577442 scopus 로고
    • Release of tyrosine from tyrosinated tubulin. Some common factors that affect this process and the assembly of tubulin
    • Hallak, M.E., Rodriguez, J.A., Barra, H.S. and Caputto, R. (1977) Release of tyrosine from tyrosinated tubulin. Some common factors that affect this process and the assembly of tubulin. FEBS Lett. 73, 147-150
    • (1977) FEBS Lett. , vol.73 , pp. 147-150
    • Hallak, M.E.1    Rodriguez, J.A.2    Barra, H.S.3    Caputto, R.4
  • 46
    • 0021752265 scopus 로고
    • Distinct populations of microtubules: Tyrosinated and nontyrosinated α tubulin are distributed differently in vivo
    • Gundersen, G.G., Kalnoski, M.H. and Bulinski, J.C. (1984) Distinct populations of microtubules: tyrosinated and nontyrosinated α tubulin are distributed differently in vivo. Cell 38, 779-789
    • (1984) Cell , vol.38 , pp. 779-789
    • Gundersen, G.G.1    Kalnoski, M.H.2    Bulinski, J.C.3
  • 50
    • 78649648936 scopus 로고    scopus 로고
    • Expression and silencing of the microtubule-associated protein Tau in breast cancer cells
    • Spicakova, T., O'Brien, M.M., Duran, G.E., Sweet-Cordero, A. and Sikic, B.I. (2010) Expression and silencing of the microtubule-associated protein Tau in breast cancer cells. Mol. Cancer Ther. 9, 2970-2981
    • (2010) Mol. Cancer Ther. , vol.9 , pp. 2970-2981
    • Spicakova, T.1    O'Brien, M.M.2    Duran, G.E.3    Sweet-Cordero, A.4    Sikic, B.I.5
  • 51
    • 0035918287 scopus 로고    scopus 로고
    • Differential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation
    • Bonnet, C., Boucher, D., Lazereg, S., Pedrotti, B., Islam, K., Denoulet, P. and Larcher, J.C. (2001) Differential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation. J. Biol. Chem. 276, 12839-12848
    • (2001) J. Biol. Chem. , vol.276 , pp. 12839-12848
    • Bonnet, C.1    Boucher, D.2    Lazereg, S.3    Pedrotti, B.4    Islam, K.5    Denoulet, P.6    Larcher, J.C.7
  • 52
    • 0029814394 scopus 로고    scopus 로고
    • Interaction of kinesin motor domains with α- and β-tubulin subunits at a tau-independent binding site. Regulation by polyglutamylation
    • Larcher, J.C., Boucher, D., Lazereg, S., Gros, F. and Denoulet, P. (1996) Interaction of kinesin motor domains with α- and β-tubulin subunits at a tau-independent binding site. Regulation by polyglutamylation. J. Biol. Chem. 271, 22117-22124
    • (1996) J. Biol. Chem. , vol.271 , pp. 22117-22124
    • Larcher, J.C.1    Boucher, D.2    Lazereg, S.3    Gros, F.4    Denoulet, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.