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Volumn 33, Issue 6, 2013, Pages 1114-1123

Tubulin acetyltransferase α TAT1 destabilizes microtubules independently of its acetylation activity

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ALPHA TUBULIN ACETYLTRANSFERASE 1; UNCLASSIFIED DRUG;

EID: 84874709998     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01044-12     Document Type: Article
Times cited : (78)

References (44)
  • 2
    • 0020540736 scopus 로고
    • Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly
    • L'Hernault SW, Rosenbaum JL. 1983. Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly. J. Cell Biol. 97:258-263.
    • (1983) J. Cell Biol. , vol.97 , pp. 258-263
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 3
    • 0023389780 scopus 로고
    • Identification of an acetylation site of Chlamydomonas alpha-tubulin
    • LeDizet M, Piperno G. 1987. Identification of an acetylation site of Chlamydomonas alpha-tubulin. Proc. Natl. Acad. Sci. U. S. A. 84:5720-5724.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 5720-5724
    • LeDizet, M.1    Piperno, G.2
  • 5
    • 77953046399 scopus 로고    scopus 로고
    • Acetylation of microtubules influences their sensitivity to severing by katanin in neurons and fibroblasts
    • Sudo H, Baas PW. 2010. Acetylation of microtubules influences their sensitivity to severing by katanin in neurons and fibroblasts. J. Neurosci. 30:7215-7226.
    • (2010) J. Neurosci. , vol.30 , pp. 7215-7226
    • Sudo, H.1    Baas, P.W.2
  • 6
    • 34250758641 scopus 로고    scopus 로고
    • HEF1-dependent Aurora A activation induces disassembly of the primary cilium
    • Pugacheva EN, Jablonski SA, Hartman TR, Henske EP, Golemis EA. 2007. HEF1-dependent Aurora A activation induces disassembly of the primary cilium. Cell 129:1351-1363.
    • (2007) Cell , vol.129 , pp. 1351-1363
    • Pugacheva, E.N.1    Jablonski, S.A.2    Hartman, T.R.3    Henske, E.P.4    Golemis, E.A.5
  • 9
    • 84866248590 scopus 로고    scopus 로고
    • MEC-17 deficiency leads to reduced alpha-tubulin acetylation and impaired migration of cortical neurons
    • Li L, Wei D, Wang Q, Pan J, Liu R, Zhang X, Bao L. 2012. MEC-17 deficiency leads to reduced alpha-tubulin acetylation and impaired migration of cortical neurons. J. Neurosci. 32:12673-12683.
    • (2012) J. Neurosci. , vol.32 , pp. 12673-12683
    • Li, L.1    Wei, D.2    Wang, Q.3    Pan, J.4    Liu, R.5    Zhang, X.6    Bao, L.7
  • 10
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E. 2003. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell 11:437-444.
    • (2003) Mol. Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 12
    • 79951819919 scopus 로고    scopus 로고
    • A novel acetylation of beta-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation
    • Chu CW, Hou F, Zhang J, Phu L, Loktev AV, Kirkpatrick DS, Jackson PK, Zhao Y, Zou H. 2011. A novel acetylation of beta-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation. Mol. Biol. Cell 22:448-456.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 448-456
    • Chu, C.W.1    Hou, F.2    Zhang, J.3    Phu, L.4    Loktev, A.V.5    Kirkpatrick, D.S.6    Jackson, P.K.7    Zhao, Y.8    Zou, H.9
  • 14
    • 78650731392 scopus 로고    scopus 로고
    • The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation
    • Shida T, Cueva JG, Xu Z, Goodman MB, Nachury MV. 2010. The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. U. S. A. 107: 21517-21522.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 21517-21522
    • Shida, T.1    Cueva, J.G.2    Xu, Z.3    Goodman, M.B.4    Nachury, M.V.5
  • 17
    • 0024536382 scopus 로고
    • Genetic control of differentiation of the Caenorhabditis elegans touch receptor neurons
    • Chalfie M, Au M. 1989. Genetic control of differentiation of the Caenorhabditis elegans touch receptor neurons. Science 243:1027-1033.
    • (1989) Science , vol.243 , pp. 1027-1033
    • Chalfie, M.1    Au, M.2
  • 23
    • 77955283527 scopus 로고    scopus 로고
    • Analysis of dynamic instability of steady-state microtubules in vitro by video-enhanced differential interference contrast microscopy with an appendix by Emin Oroudjev
    • Yenjerla M, Lopus M, Wilson L. 2010. Analysis of dynamic instability of steady-state microtubules in vitro by video-enhanced differential interference contrast microscopy with an appendix by Emin Oroudjev. Methods Cell Biol. 95:189-206.
    • (2010) Methods Cell Biol. , vol.95 , pp. 189-206
    • Yenjerla, M.1    Lopus, M.2    Wilson, L.3
  • 25
    • 0022399572 scopus 로고
    • Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms
    • Piperno G, Fuller MT. 1985. Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms. J. Cell Biol. 101:2085-2094.
    • (1985) J. Cell Biol. , vol.101 , pp. 2085-2094
    • Piperno, G.1    Fuller, M.T.2
  • 26
    • 33845666508 scopus 로고    scopus 로고
    • Eukaryotic domain of unknown function DUF738 belongs to Gcn5-related N-acetyltransferase superfamily
    • Steczkiewicz K, Kinch L, Grishin NV, Rychlewski L, Ginalski K. 2006. Eukaryotic domain of unknown function DUF738 belongs to Gcn5-related N-acetyltransferase superfamily. Cell Cycle 5:2927-2930.
    • (2006) Cell Cycle , vol.5 , pp. 2927-2930
    • Steczkiewicz, K.1    Kinch, L.2    Grishin, N.V.3    Rychlewski, L.4    Ginalski, K.5
  • 30
    • 0037448671 scopus 로고    scopus 로고
    • Cell biology: tubulin acetylation and cell motility
    • Palazzo A, Ackerman B, Gundersen GG. 2003. Cell biology: tubulin acetylation and cell motility. Nature 421:230.
    • (2003) Nature , vol.421 , pp. 230
    • Palazzo, A.1    Ackerman, B.2    Gundersen, G.G.3
  • 32
    • 77957198722 scopus 로고    scopus 로고
    • Quantitative image analysis identifies pVHL as a key regulator of microtubule dynamic instability
    • Thoma CR, Matov A, Gutbrodt KL, Hoerner CR, Smole Z, Krek W, Danuser G. 2010. Quantitative image analysis identifies pVHL as a key regulator of microtubule dynamic instability. J. Cell Biol. 190:991-1003.
    • (2010) J. Cell Biol. , vol.190 , pp. 991-1003
    • Thoma, C.R.1    Matov, A.2    Gutbrodt, K.L.3    Hoerner, C.R.4    Smole, Z.5    Krek, W.6    Danuser, G.7
  • 33
    • 78951470412 scopus 로고    scopus 로고
    • Distinct ECM mechanosensing pathways regulate microtubule dynamics to control endothelial cell branching morphogenesis
    • Myers KA, Applegate KT, Danuser G, Fischer RS, Waterman CM. 2011. Distinct ECM mechanosensing pathways regulate microtubule dynamics to control endothelial cell branching morphogenesis. J. Cell Biol. 192:321-334.
    • (2011) J. Cell Biol. , vol.192 , pp. 321-334
    • Myers, K.A.1    Applegate, K.T.2    Danuser, G.3    Fischer, R.S.4    Waterman, C.M.5
  • 36
    • 33846374117 scopus 로고    scopus 로고
    • Catalytic mechanism of a MYST family histone acetyltransferase
    • Berndsen CE, Albaugh BN, Tan S, Denu JM. 2007. Catalytic mechanism of a MYST family histone acetyltransferase. Biochemistry 46:623-629.
    • (2007) Biochemistry , vol.46 , pp. 623-629
    • Berndsen, C.E.1    Albaugh, B.N.2    Tan, S.3    Denu, J.M.4
  • 38
    • 0036830560 scopus 로고    scopus 로고
    • The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate
    • Yan Y, Harper S, Speicher DW, Marmorstein R. 2002. The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate. Nat. Struct. Biol. 9:862-869.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 862-869
    • Yan, Y.1    Harper, S.2    Speicher, D.W.3    Marmorstein, R.4
  • 39
    • 57049120143 scopus 로고    scopus 로고
    • Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function
    • Wang L, Tang Y, Cole PA, Marmorstein R. 2008. Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function. Curr. Opin. Struct. Biol. 18:741-747.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 741-747
    • Wang, L.1    Tang, Y.2    Cole, P.A.3    Marmorstein, R.4
  • 40
    • 84870316474 scopus 로고    scopus 로고
    • Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA
    • Taschner M, Vetter M, Lorentzen E. 2012. Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA. Proc. Natl. Acad. Sci. U. S. A. 109:19649-19654.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 19649-19654
    • Taschner, M.1    Vetter, M.2    Lorentzen, E.3
  • 41
    • 84870342617 scopus 로고    scopus 로고
    • Structure of the alpha-tubulin acetyltransferase, alphaTAT1, and implications for tubulin-specific acetylation
    • Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R. 2012. Structure of the alpha-tubulin acetyltransferase, alphaTAT1, and implications for tubulin-specific acetylation. Proc. Natl. Acad. Sci. U. S. A. 109: 19655-19660.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 19655-19660
    • Friedmann, D.R.1    Aguilar, A.2    Fan, J.3    Nachury, M.V.4    Marmorstein, R.5
  • 42
    • 0022452231 scopus 로고
    • The acetylation of alphatubulin and its relationship to the assembly and disassembly of microtubules
    • Maruta H, Greer K, Rosenbaum JL. 1986. The acetylation of alphatubulin and its relationship to the assembly and disassembly of microtubules. J. Cell Biol. 103:571-579.
    • (1986) J. Cell Biol. , vol.103 , pp. 571-579
    • Maruta, H.1    Greer, K.2    Rosenbaum, J.L.3
  • 43
    • 0029035184 scopus 로고
    • Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila
    • Gaertig J, Cruz MA, Bowen J, Gu L, Pennock DG, Gorovsky MA. 1995. Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila. J. Cell Biol. 129:1301-1310.
    • (1995) J. Cell Biol. , vol.129 , pp. 1301-1310
    • Gaertig, J.1    Cruz, M.A.2    Bowen, J.3    Gu, L.4    Pennock, D.G.5    Gorovsky, M.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.