메뉴 건너뛰기




Volumn 109, Issue 48, 2012, Pages 19515-19516

α-Tubulin acetylation from the inside out

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; ALPHA TUBULIN ACETYLTRANSFERASE; ASPARAGINE; CYSTEINE; GLUTAMINE; LYSINE; UNCLASSIFIED DRUG;

EID: 84870380891     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1217594109     Document Type: Note
Times cited : (26)

References (17)
  • 1
    • 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
  • 2
    • 81855196008 scopus 로고    scopus 로고
    • Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions
    • Janke C, Bulinski JC (2011) Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions. Nat Rev Mol Cell Biol 12(12):773-786.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.12 , pp. 773-786
    • Janke, C.1    Bulinski, J.C.2
  • 3
    • 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
  • 4
    • 84866248590 scopus 로고    scopus 로고
    • MEC-17 deficiency leads to reduced α-tubulin acetylation and impaired migration of cortical neurons
    • Li L, et al. (2012) MEC-17 deficiency leads to reduced α-tubulin acetylation and impaired migration of cortical neurons. J Neurosci 32(37):12673-12683.
    • (2012) J Neurosci , vol.32 , Issue.37 , pp. 12673-12683
    • Li, L.1
  • 5
    • 84857426309 scopus 로고    scopus 로고
    • Ciliary and flagellar structure and function-their regulations by posttranslational modifications of axonemal tubulin
    • Konno A, Setou M, Ikegami K (2012) Ciliary and flagellar structure and function-their regulations by posttranslational modifications of axonemal tubulin. Int Rev Cell Mol Biol 294:133-170.
    • (2012) Int Rev Cell Mol Biol , vol.294 , pp. 133-170
    • Konno, A.1    Setou, M.2    Ikegami, K.3
  • 6
    • 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
  • 7
    • 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
  • 8
    • 84870342617 scopus 로고    scopus 로고
    • Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation
    • Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R (2012) Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc Natl Acad Sci USA 109:19655-19660.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 19655-19660
    • Friedmann, D.R.1    Aguilar, A.2    Fan, J.3    Nachury, M.V.4    Marmorstein, R.5
  • 9
    • 84870316474 scopus 로고    scopus 로고
    • Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA
    • Taschner M, Vetter M, Lorentzen E (2012) Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA. Proc Natl Acad Sci USA 109:19649-19654.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 19649-19654
    • Taschner, M.1    Vetter, M.2    Lorentzen, E.3
  • 10
    • 84862658847 scopus 로고    scopus 로고
    • Post-translational acetylation of α-tubulin constrains protofilament number in native microtubules
    • Cueva JG, Hsin J, Huang KC, Goodman MB (2012) Post-translational 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
  • 11
    • 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
  • 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
    • 77953879123 scopus 로고    scopus 로고
    • The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics membrane proteins to cilia
    • Jin H, et al. (2010) The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics membrane proteins to cilia. Cell 141(7):1208-1219.
    • (2010) Cell , vol.141 , Issue.7 , pp. 1208-1219
    • Jin, H.1
  • 14
    • 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(6):741-747.
    • (2008) Curr Opin Struct Biol , vol.18 , Issue.6 , pp. 741-747
    • Wang, L.1    Tang, Y.2    Cole, P.A.3    Marmorstein, R.4
  • 15
    • 0141992114 scopus 로고    scopus 로고
    • Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase
    • Clements A, et al. (2003) Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase. Mol Cell 12(2):461-473.
    • (2003) Mol Cell , vol.12 , Issue.2 , pp. 461-473
    • Clements, A.1
  • 16
    • 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
  • 17
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.