Home LiteratureArticle Details
PMID: 19920250 Published · epublish English Journal Article Research Support, N.I.H., Extramural

Acetylation goes global: the emergence of acetylation biology.

Science signaling ·Vol. 2 ·No. 97 ·2009-11-17 ·Pages pe76

Norris KL, Lee JY, Yao TP

Abstract

For the first 30 years since its discovery, reversible protein acetylation has been studied and understood almost exclusively in the context of histone modification and gene transcription. With the discovery of non-histone acetylated proteins and acetylation-modifying enzymes in cellular compartments outside the nucleus, the regulatory potential of reversible acetylation has slowly been recognized in the last decade. However, the scope of protein acetylation involvement in complex biological processes remains uncertain. The recent development of new technology has enabled, for the first time, the identification and quantification of the acetylome, acetylation events at the whole-proteome level. These efforts have uncovered a stunning complexity of the acetylome that potentially rivals that of the phosphoproteome. The remarkably ubiquitous and conserved nature of protein acetylation revealed by these new studies suggests the regulatory power of this dynamic modification. The establishment of comprehensive acetylomes will change the landscape of protein acetylation, where an exciting research frontier awaits.

MeSH Terms
Acetylation Acetyltransferases/metabolism Animals Histone Deacetylases/metabolism Humans Lysine/metabolism Models, Biological Protein Processing, Post-Translational Proteins/metabolism Proteomics/methods,trends Signal Transduction
Chemicals
Proteins Acetyltransferases Histone Deacetylases Lysine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Norris Kristi L
Department of Pharmacology and Cancer Biology, Duke University, Durham, NC 27710, USA.
Lee Joo-Yong
Yao Tso-Pang
References (35)
35 references, click to expand
  1. PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites.
    Genome Biol. 2007;8(11):R250 PMID: 18039369
  2. Histone deacetylase inhibitors in inflammatory disease.
    Curr Top Med Chem. 2009;9(3):309-19 PMID: 19355993
  3. Translating the histone code.
    Science. 2001 Aug 10;293(5532):1074-80 PMID: 11498575
  4. SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle.
    Cell. 2009 May 1;137(3):560-70 PMID: 19410549
  5. Functional and quantitative proteomics using SILAC.
    Nat Rev Mol Cell Biol. 2006 Dec;7(12):952-8 PMID: 17139335
  6. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae.
    Science. 2000 Sep 22;289(5487):2126-8 PMID: 11000115
  7. Lysine acetylation targets protein complexes and co-regulates major cellular functions.
    Science. 2009 Aug 14;325(5942):834-40 PMID: 19608861
  8. SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria.
    Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13653-8 PMID: 12374852
  9. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2.
    Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10224-10229 PMID: 16788062
  10. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain.
    Cell. 1997 Aug 22;90(4):595-606 PMID: 9288740
  11. The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase.
    J Cell Biol. 2002 Aug 19;158(4):647-57 PMID: 12186850
  12. HDAC6 is a microtubule-associated deacetylase.
    Nature. 2002 May 23;417(6887):455-8 PMID: 12024216
  13. AcK-knowledge reversible acetylation.
    Sci STKE. 2004 Aug 03;2004(245):pe42 PMID: 15304664
  14. A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors.
    Proc Natl Acad Sci U S A. 1999 Apr 13;96(8):4592-7 PMID: 10200307
  15. Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone.
    J Biol Chem. 1968 Oct 10;243(19):5018-22 PMID: 5679978
  16. Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation.
    Mol Cell. 2004 Jan 30;13(2):251-63 PMID: 14759370
  17. Histone deacetylase inhibitors: Potential in cancer therapy.
    J Cell Biochem. 2009 Jul 1;107(4):600-8 PMID: 19459166
  18. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors.
    J Biol Chem. 2005 Jul 22;280(29):26729-34 PMID: 15937340
  19. Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.
    Science. 2002 Dec 20;298(5602):2390-2 PMID: 12493915
  20. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases.
    Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10230-10235 PMID: 16790548
  21. HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor.
    Mol Cell. 2005 May 27;18(5):601-7 PMID: 15916966
  22. Therapeutic application of histone deacetylase inhibitors for central nervous system disorders.
    Nat Rev Drug Discov. 2008 Oct;7(10):854-68 PMID: 18827828
  23. Coactivator and corepressor complexes in nuclear receptor function.
    Curr Opin Genet Dev. 1999 Apr;9(2):140-7 PMID: 10322133
  24. 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. 1985 Dec;101(6):2085-94 PMID: 2415535
  25. Intrinsic protein disorder, amino acid composition, and histone terminal domains.
    J Biol Chem. 2006 Jan 27;281(4):1853-6 PMID: 16301309
  26. Calorie restriction alters mitochondrial protein acetylation.
    Aging Cell. 2009 Sep;8(5):604-6 PMID: 19594485
  27. Histone H2A.Z acetylation modulates an essential charge patch.
    Mol Cell. 2001 Jun;7(6):1329-35 PMID: 11430834
  28. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
    Mol Cell. 2006 Aug;23(4):607-18 PMID: 16916647
  29. Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
    Mol Cell Proteomics. 2009 Feb;8(2):215-25 PMID: 18723842
  30. Acetylation: a regulatory modification to rival phosphorylation?
    EMBO J. 2000 Mar 15;19(6):1176-9 PMID: 10716917
  31. VopA inhibits ATP binding by acetylating the catalytic loop of MAPK kinases.
    J Biol Chem. 2007 Nov 23;282(47):34299-305 PMID: 17881352
  32. Identification of novel isoform-selective inhibitors within class I histone deacetylases.
    J Pharmacol Exp Ther. 2003 Nov;307(2):720-8 PMID: 12975486
  33. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
    Cell. 2006 Nov 3;127(3):635-48 PMID: 17081983
  34. Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine.
    Biochemistry. 1985 Jan 15;24(2):473-8 PMID: 3919761
  35. Lysine acetylation: codified crosstalk with other posttranslational modifications.
    Mol Cell. 2008 Aug 22;31(4):449-461 PMID: 18722172
Article Info
Journal
Science signaling
Abbr.
Sci Signal
ISSN
1937-9145
Published
2009-11-17
Epub
2009-00-17
Pages
pe76
Language
English
Region
United States
NLM ID
101465400
PMCID
PMC2812806
Subset
IM
Grants
NINDS NIH HHS · NS054022 · United States
NIAMS NIH HHS · R01 AR055613-02 · United States
NINDS NIH HHS · R01 NS054022-04 · United States
NIAMS NIH HHS · AR055613 · United States
NINDS NIH HHS · R01 NS054022 · United States
NIAMS NIH HHS · R01 AR055613 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]