|
 |
|
|
|
EMBO reports 8, 6, 556–562 (2007)
doi:10.1038/sj.embor.7400977
Metabolism, cytoskeleton and cellular signalling in the grip of protein N - and O-acetylation
Xiang-Jiao Yang & Serge Grégoire
|
|
|
|
Molecular Oncology Group, Department of Medicine, Royal Victoria Hospital, Room H5.41, McGill University Health Centre, 687 Pine Avenue West, Montréal, Québec H3A 1A1, Canada
To whom correspondence should be addressed
Xiang-Jiao Yang Tel: +1 514 934 1934 ext. 34490; Fax: +1 514 843 1478;
xiang-jiao.yang@mcgill.ca
Received 15 February 2007; Accepted 27 March 2007.
|
|
|
|
Abstract
Acetylation of the  -amino group of lysine residues (N-acetylation) is a reversible post-translational modification with the potential to rival phosphorylation. In addition to histones and many transcription factors such as p53, regulators of DNA repair, replication and recombination are subject to N-acetylation. This modification is also important for governing the activities of various enzymes, including histone acetyltransferases, histone deacetylases, bacterial and mammalian acetyl-CoA synthases, kinases, phosphatases, the ubiquitin ligase murine double minute 2 and the chaperonin heat shock protein 90. Furthermore, lysine acetylation occurs in cellular structure proteins such as  -tubulin, actin, cortactin and p120 catenin. Strikingly, the Yersinia outer protein YopJ promotes O-acetylation of crucial serine and threonine residues that are required for activation of the MAPK/ERK kinase and I B kinase families, which precludes their phosphorylation and blocks signal transduction. Thus, N- and O-acetylation are becoming recognized as two prominent mechanisms for regulating protein functions in diverse organisms.
|
 |
|
Top of page MORE ARTICLES LIKE THIS These links to content published by NPG are automatically generated | |
|
top  |
|
|
|
