메뉴 건너뛰기




Volumn 109, Issue 48, 2012, Pages 19655-19660

Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation

Author keywords

Crystallography; Enzymology

Indexed keywords

ALANINE; ALPHA TUBULIN; ALPHA TUBULIN ACETYLTRANSFERASE 1; ASPARTIC ACID; CYSTEINE; HISTONE ACETYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 84870342617     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1209357109     Document Type: Article
Times cited : (62)

References (35)
  • 1
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • Glozak MA, Sengupta N, Zhang X, Seto E (2005) Acetylation and deacetylation of non-histone proteins. Gene 363:15-23.
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 3
    • 34547897023 scopus 로고    scopus 로고
    • Histone deacetylases and cancer
    • Glozak MA, Seto E (2007) Histone deacetylases and cancer. Oncogene 26(37): 5420-5432.
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5420-5432
    • Glozak, M.A.1    Seto, E.2
  • 4
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides T (2000) Acetylation: A regulatory modification to rival phosphorylation? EMBO J 19(6):1176-1179.
    • (2000) EMBO J , vol.19 , Issue.6 , pp. 1176-1179
    • Kouzarides, T.1
  • 5
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C, et al. (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325(5942):834-840.
    • (2009) Science , vol.325 , Issue.5942 , pp. 834-840
    • Choudhary, C.1
  • 6
    • 0021993649 scopus 로고
    • Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine
    • L'Hernault SW, Rosenbaum JL (1985) Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine. Biochemistry 24(2):473-478.
    • (1985) Biochemistry , vol.24 , Issue.2 , pp. 473-478
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 7
    • 0022452231 scopus 로고
    • The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules
    • Maruta H, Greer K, Rosenbaum JL (1986) The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules. J Cell Biol 103(2): 571-579.
    • (1986) J Cell Biol , vol.103 , Issue.2 , pp. 571-579
    • Maruta, H.1    Greer, K.2    Rosenbaum, J.L.3
  • 8
    • 0023293040 scopus 로고
    • Microtubules containing acetylated alphatubulin in mammalian cells in culture
    • Piperno G, LeDizet M, Chang XJ (1987) Microtubules containing acetylated alphatubulin in mammalian cells in culture. J Cell Biol 104(2):289-302.
    • (1987) J Cell Biol , vol.104 , Issue.2 , pp. 289-302
    • Piperno, G.1    LeDizet, M.2    Chang, X.J.3
  • 9
    • 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 USA 107(50):21517-21522.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.50 , pp. 21517-21522
    • Shida, T.1    Cueva, J.G.2    Xu, Z.3    Goodman, M.B.4    Nachury, M.V.5
  • 10
    • 77956525850 scopus 로고    scopus 로고
    • MEC-17 is an alpha-tubulin acetyltransferase
    • Akella JS, et al. (2010) MEC-17 is an alpha-tubulin acetyltransferase. Nature 467(7312): 218-222.
    • (2010) Nature , vol.467 , Issue.7312 , pp. 218-222
    • Akella, J.S.1
  • 11
    • 33750618516 scopus 로고    scopus 로고
    • Microtubule acetylation promotes kinesin-1 binding and transport
    • Reed NA, et al. (2006) Microtubule acetylation promotes kinesin-1 binding and transport. Curr Biol 16(21):2166-2172.
    • (2006) Curr Biol , vol.16 , Issue.21 , pp. 2166-2172
    • Reed, N.A.1
  • 12
    • 57049171416 scopus 로고    scopus 로고
    • A BBSome subunit links ciliogenesis, microtubule stability, and acetylation
    • Loktev AV, et al. (2008) A BBSome subunit links ciliogenesis, microtubule stability, and acetylation. Dev Cell 15(6):854-865.
    • (2008) Dev Cell , vol.15 , Issue.6 , pp. 854-865
    • Loktev, A.V.1
  • 13
    • 0033517354 scopus 로고    scopus 로고
    • Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide
    • Rojas JR, et al. (1999) Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide. Nature 401(6748):93-98.
    • (1999) Nature , vol.401 , Issue.6748 , pp. 93-98
    • Rojas, J.R.1
  • 14
    • 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(11):862-869.
    • (2002) Nat Struct Biol , vol.9 , Issue.11 , pp. 862-869
    • Yan, Y.1    Harper, S.2    Speicher, D.W.3    Marmorstein, R.4
  • 15
    • 84855341934 scopus 로고    scopus 로고
    • MYST protein acetyltransferase activity requires active site lysine autoacetylation
    • Yuan H, et al. (2012) MYST protein acetyltransferase activity requires active site lysine autoacetylation. EMBO J 31(1):58-70.
    • (2012) EMBO J , vol.31 , Issue.1 , pp. 58-70
    • Yuan, H.1
  • 17
    • 0033010021 scopus 로고    scopus 로고
    • Melatonin biosynthesis: The structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism
    • Hickman AB, Klein DC, Dyda F (1999) Melatonin biosynthesis: The structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism. Mol Cell 3(1):23-32.
    • (1999) Mol Cell , vol.3 , Issue.1 , pp. 23-32
    • Hickman, A.B.1    Klein, D.C.2    Dyda, F.3
  • 18
    • 80054694313 scopus 로고    scopus 로고
    • Structure of a ternary Naa50p (NAT5/ SAN) N-terminal acetyltransferase complex reveals the molecular basis for substratespecific acetylation
    • Liszczak G, Arnesen T, Marmorstein R (2011) Structure of a ternary Naa50p (NAT5/ SAN) N-terminal acetyltransferase complex reveals the molecular basis for substratespecific acetylation. J Biol Chem 286(42):37002-37010.
    • (2011) J Biol Chem , vol.286 , Issue.42 , pp. 37002-37010
    • Liszczak, G.1    Arnesen, T.2    Marmorstein, R.3
  • 19
    • 39149109887 scopus 로고    scopus 로고
    • The structural basis of protein acetylation by the p300/CBP transcriptional coactivator
    • Liu X, et al. (2008) The structural basis of protein acetylation by the p300/CBP transcriptional coactivator. Nature 451(7180):846-850.
    • (2008) Nature , vol.451 , Issue.7180 , pp. 846-850
    • Liu, X.1
  • 20
    • 0034664244 scopus 로고    scopus 로고
    • The 4 A X-ray structure of a tubulin:stathmin-like domain complex
    • Gigant B, et al. (2000) The 4 A X-ray structure of a tubulin:stathmin- like domain complex. Cell 102(6):809-816.
    • (2000) Cell , vol.102 , Issue.6 , pp. 809-816
    • Gigant, B.1
  • 21
    • 46449118856 scopus 로고    scopus 로고
    • Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP
    • Tang Y, et al. (2008) Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP. Nat Struct Mol Biol 15(9):998.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.9 , pp. 998
    • Tang, Y.1
  • 22
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • Spange S, Wagner T, Heinzel T, Krämer OH (2009) Acetylation of non-histone proteins modulates cellular signalling at multiple levels. Int J Biochem Cell Biol 41(1):185-198.
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.1 , pp. 185-198
    • Spange, S.1    Wagner, T.2    Heinzel, T.3    Krämer, O.H.4
  • 23
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y (1996) The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87(5):953-959.
    • (1996) Cell , vol.87 , Issue.5 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 24
    • 79953712902 scopus 로고    scopus 로고
    • MYST-family histone acetyltransferases: Beyond chromatin
    • Sapountzi V, Côté J (2011) MYST-family histone acetyltransferases: Beyond chromatin. Cell Mol Life Sci 68(7):1147-1156.
    • (2011) Cell Mol Life Sci , vol.68 , Issue.7 , pp. 1147-1156
    • Sapountzi, V.1    Côté, J.2
  • 25
    • 33846818840 scopus 로고    scopus 로고
    • Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56
    • Driscoll R, Hudson A, & Jackson SP (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-652.
    • (2007) Science , vol.315 , Issue.5812 , pp. 649-652
    • Driscoll, R.1    Hudson, A.2    Jackson, S.P.3
  • 26
    • 0033605238 scopus 로고    scopus 로고
    • Expanded lysine acetylation specificity of Gcn5 in native complexes
    • Grant PA, et al. (1999) Expanded lysine acetylation specificity of Gcn5 in native complexes. J Biol Chem 274(9):5895-5900.
    • (1999) J Biol Chem , vol.274 , Issue.9 , pp. 5895-5900
    • Grant, P.A.1
  • 27
    • 84862658847 scopus 로고    scopus 로고
    • Posttranslational acetylation of α-tubulin constrains protofilament number in native microtubules
    • Cueva JG, Hsin J, Huang KC, Goodman MB (2012) Posttranslational acetylation of α-tubulin constrains protofilament number in native microtubules. Curr Biol 22(12): 1066-1074.
    • (2012) Curr Biol , vol.22 , Issue.12 , pp. 1066-1074
    • Cueva, J.G.1    Hsin, J.2    Huang, K.C.3    Goodman, M.B.4
  • 28
    • 84862690126 scopus 로고    scopus 로고
    • Genetically separable functions of the MEC-17 tubulin acetyltransferase affect microtubule organization
    • Topalidou I, et al. (2012) Genetically separable functions of the MEC-17 tubulin acetyltransferase affect microtubule organization. Curr Biol 22(12):1057-1065.
    • (2012) Curr Biol , vol.22 , Issue.12 , pp. 1057-1065
    • Topalidou, I.1
  • 30
    • 0037413708 scopus 로고    scopus 로고
    • Repeat motifs of tau bind to the insides of microtubules in the absence of taxol
    • Kar S, Fan J, Smith MJ, Goedert M, Amos LA (2003) Repeat motifs of tau bind to the insides of microtubules in the absence of taxol. EMBO J 22(1):70-77.
    • (2003) EMBO J , vol.22 , Issue.1 , pp. 70-77
    • Kar, S.1    Fan, J.2    Smith, M.J.3    Goedert, M.4    Amos, L.A.5
  • 31
    • 84981860375 scopus 로고
    • Role of chance observations in chemotherapy: Vinca rosea
    • Noble RL, Beer CT, Cutts JH (1958) Role of chance observations in chemotherapy: Vinca rosea. Ann N Y Acad Sci 76(3):882-894.
    • (1958) Ann N Y Acad Sci , vol.76 , Issue.3 , pp. 882-894
    • Noble, R.L.1    Beer, C.T.2    Cutts, J.H.3
  • 32
    • 0015211527 scopus 로고
    • Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia
    • Wani MC, Taylor HL, Wall ME, Coggon P, McPhail AT (1971) Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia. J Am Chem Soc 93(9):2325-2327.
    • (1971) J Am Chem Soc , vol.93 , Issue.9 , pp. 2325-2327
    • Wani, M.C.1    Taylor, H.L.2    Wall, M.E.3    Coggon, P.4    McPhail, A.T.5
  • 33
    • 28844499921 scopus 로고    scopus 로고
    • Microtubule interactions with chemically diverse stabilizing agents: Thermodynamics of binding to the paclitaxel site predicts cytotoxicity
    • Buey RM, et al. (2005) Microtubule interactions with chemically diverse stabilizing agents: Thermodynamics of binding to the paclitaxel site predicts cytotoxicity. Chem Biol 12(12):1269-1279.
    • (2005) Chem Biol , vol.12 , Issue.12 , pp. 1269-1279
    • Buey, R.M.1
  • 34
    • 0033213979 scopus 로고    scopus 로고
    • Additivity of dilantin and vinblastine inhibitory effects on microtubule assembly
    • Lobert S, Ingram JW, Correia JJ (1999) Additivity of dilantin and vinblastine inhibitory effects on microtubule assembly. Cancer Res 59(19):4816-4822.
    • (1999) Cancer Res , vol.59 , Issue.19 , pp. 4816-4822
    • Lobert, S.1    Ingram, J.W.2    Correia, J.J.3
  • 35
    • 41549104608 scopus 로고    scopus 로고
    • Anti-tumor activity of capecitabine and vinorelbine in patients with anthracycline- and taxane-pretreated metastatic breast cancer: Findings from the EORTC 10001 randomized phase II trial
    • Pajk B, et al. (2008) Anti-tumor activity of capecitabine and vinorelbine in patients with anthracycline- and taxane-pretreated metastatic breast cancer: Findings from the EORTC 10001 randomized phase II trial. Breast 17(2):180-185.
    • (2008) Breast , vol.17 , Issue.2 , pp. 180-185
    • Pajk, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.