MYST-family histone acetyltransferases: beyond chromatin.

Cell Mol Life Sci 2011 Apr 4;68(7):1147-56. Epub 2010 Dec 4.

Laval University Cancer Research Center, Hôtel-Dieu de Québec (CHUQ), 9 McMahon Street, Quebec City, QC, G1R 2J6, Canada.

Covalently modifying a protein has proven to be a powerful mechanism of functional regulation. N-epsilon acetylation of lysine residues was initially discovered on histones and has been studied extensively in the context of chromatin and DNA metabolism, such as transcription, replication and repair. However, recent research shows that acetylation is more widespread than initially thought and that it regulates various nuclear as well as cytoplasmic and mitochondrial processes. In this review, we present the multitude of non-histone proteins targeted by lysine acetyltransferases of the large and conserved MYST family, and known functional consequences of this acetylation. Substrates of MYST enzymes include factors involved in transcription, heterochromatin formation and cell cycle, DNA repair proteins, gluconeogenesis enzymes and finally subunits of MYST protein complexes themselves. Discovering novel substrates of MYST proteins is pivotal for the understanding of the diverse functions of these essential acetyltransferases in nuclear processes, signaling, stress response and metabolism.

Download full-text PDF

Source
http://dx.doi.org/10.1007/s00018-010-0599-9DOI Listing
April 2011
15 Reads

Publication Analysis

Top Keywords

substrates myst
8
formation cell
4
initially thought
4
cell cycle
4
thought regulates
4
heterochromatin formation
4
involved transcription
4
nuclear well
4
transcription heterochromatin
4
regulates nuclear
4
widespread initially
4
acetylation widespread
4
repair proteins
4
metabolism transcription
4
proteins gluconeogenesis
4
dna metabolism
4
transcription replication
4
dna repair
4
cycle dna
4
repair acetylation
4

References

(Supplied by CrossRef)

CD Allis et al.
Cell 2007

KT Smith et al.
Nat Biotechnol 2009

C Choudhary et al.
Science 2009

H Iwabata et al.
Proteomics 2005

SC Kim et al.
Mol Cell 2006

BJ Yu et al.
J Microbiol Biotechnol 2008

S Zhao et al.
Science 2010

SD Taverna et al.
Nat Struct Mol Biol 2007

JA Latham et al.
Nat Struct Mol Biol 2007

VG Allfrey et al.
Proc Natl Acad Sci USA 1964

D Ivanov et al.
Curr Biol 2002

Similar Publications