Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Sci. STKE, 10 August 2004
Vol. 2004, Issue 245, p. pe42
[DOI: 10.1126/stke.2452004pe42]

PERSPECTIVES

AcK-knowledge Reversible Acetylation

Todd Cohen and Tso-Pang Yao*

Department of Pharmacology and Cancer Biology, Duke University, Durham, NC 27710, USA.

Abstract: In 1966, the histone was identified as the first protein subject to reversible acetylation. The ensuing 30 years of research on histone acetylation has been critical for elucidating how gene transcription and chromatin remodeling are regulated at the molecular level. This central focus on histones, however, has also restricted our understanding of reversible acetylation, and therefore the enzymes that catalyze this reaction, to cellular processes predominantly associated with chromatin. The study of reversible acetylation has become more or less synonymous with histone acetylation. Recent developments—including increased ability to detect acetylated proteins, the characterization of novel acetyltransferases and deacetylases, and the identification of specific inhibitors for these enzymes—have revealed that this histone-central paradigm probably reflects only a fraction of the cellular processes regulated by reversible acetylation. New studies have uncovered unexpected roles for reversible acetylation in many diverse areas, thereby establishing protein acetylation as a highly versatile signaling modification that has functions beyond gene transcription and chromatin remodeling.

*Corresponding author. E-mail: yao00001{at}mc.duke.edu

Citation: T. Cohen, T.-P. Yao, AcK-knowledge Reversible Acetylation. Sci. STKE 2004, pe42 (2004).

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Identification of Lysine Succinylation Substrates and the Succinylation Regulatory Enzyme CobB in Escherichia coli.
G. Colak, Z. Xie, A. Y. Zhu, L. Dai, Z. Lu, Y. Zhang, X. Wan, Y. Chen, Y. H. Cha, H. Lin, et al. (2013)
Mol. Cell. Proteomics 12, 3509-3520
   Abstract »    Full Text »    PDF »
Posttranslational modifications in histones underlie heat acclimation-mediated cytoprotective memory.
A. Tetievsky and M. Horowitz (2010)
J Appl Physiol 109, 1552-1561
   Abstract »    Full Text »    PDF »
Acetylation Goes Global: The Emergence of Acetylation Biology.
K. L. Norris, J.-Y. Lee, and T.-P. Yao (2009)
Science Signaling 2, pe76
   Abstract »    Full Text »    PDF »
Lysine Acetylation Is a Highly Abundant and Evolutionarily Conserved Modification in Escherichia Coli.
J. Zhang, R. Sprung, J. Pei, X. Tan, S. Kim, H. Zhu, C.-F. Liu, N. V. Grishin, and Y. Zhao (2009)
Mol. Cell. Proteomics 8, 215-225
   Abstract »    Full Text »    PDF »
HDAC6 Is Required for Epidermal Growth Factor-induced {beta}-Catenin Nuclear Localization.
Y. Li, X. Zhang, R. D. Polakiewicz, T.-P. Yao, and M. J. Comb (2008)
J. Biol. Chem. 283, 12686-12690
   Abstract »    Full Text »    PDF »
Histone Deacetylase 6 Regulates Growth Factor-Induced Actin Remodeling and Endocytosis.
Y.-s. Gao, C. C. Hubbert, J. Lu, Y.-S. Lee, J.-Y. Lee, and T.-P. Yao (2007)
Mol. Cell. Biol. 27, 8637-8647
   Abstract »    Full Text »    PDF »
Histone Deacetylase 3 Interacts with and Deacetylates Myocyte Enhancer Factor 2.
S. Gregoire, L. Xiao, J. Nie, X. Zhang, M. Xu, J. Li, J. Wong, E. Seto, and X.-J. Yang (2007)
Mol. Cell. Biol. 27, 1280-1295
   Abstract »    Full Text »    PDF »
Positive and Negative Regulation of the Innate Antiviral Response and Beta Interferon Gene Expression by Deacetylation.
I. Nusinzon and C. M. Horvath (2006)
Mol. Cell. Biol. 26, 3106-3113
   Abstract »    Full Text »    PDF »
Identification of the Ankyrin Repeat Proteins ANKRA and RFXANK as Novel Partners of Class IIa Histone Deacetylases.
A. H. Wang, S. Gregoire, E. Zika, L. Xiao, C. S. Li, H. Li, K. L. Wright, J. P. Ting, and X.-J. Yang (2005)
J. Biol. Chem. 280, 29117-29127
   Abstract »    Full Text »    PDF »
Transforming activity of MECT1-MAML2 fusion oncoprotein is mediated by constitutive CREB activation.
L. Wu, J. Liu, P. Gao, M. Nakamura, Y. Cao, H. Shen, and J. D. Griffin (2005)
EMBO J. 24, 2391-2402
   Abstract »    Full Text »    PDF »
Class II Histone Deacetylases: from Sequence to Function, Regulation, and Clinical Implication.
X.-J. Yang and S. Gregoire (2005)
Mol. Cell. Biol. 25, 2873-2884
   Full Text »    PDF »

To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882