TY - JOUR
T1 - A newly discovered post-translational modification - the acetylation of serine and threonine residues
AU - Mukherjee, Sohini
AU - Hao, Yi Heng
AU - Orth, Kim
N1 - Funding Information:
We thank Yuh-Min Chook, Kristen Lynch, Meg Phillips and George DeMartino for insightful discussions and critical reading of the manuscript. We also thank the members of the Orth laboratory, Amy Haughey and Wanda Simpson for their generous support and assistance. K.O., S.M. and Y.I.H. are supported by grants from NIH/NIAID (R01-AI056404; R21-DK072134) and the Welch Research Foundation (I-1561; I-1128). K.O is a Burroughs Wellcome Investigator in Pathogenesis of Infectious Disease and W.W. Caruth, Jr. Biomedical Scholar.
PY - 2007/5
Y1 - 2007/5
N2 - Recent studies on a bacterial virulence factor, YopJ of Yersinia, have led to the realization that the acetylation of serine and threonine residues could be an important form of post-translational modification in eukaryotes. Although the identification of the machinery used for the addition and removal of acetyl groups on serine or threonine residues is in its infancy, the enzymes thus-far studied provide early insight into the mechanism of this newly discovered post-translational modification, and hint at its potential importance. For example, acetylation can compete with phosphorylation targeted to the same residues and could, therefore, alter the course of signaling pathways. What are the implications for signal transduction in eukaryotes and how widespread could acetylation of serine and threonine prove to be?
AB - Recent studies on a bacterial virulence factor, YopJ of Yersinia, have led to the realization that the acetylation of serine and threonine residues could be an important form of post-translational modification in eukaryotes. Although the identification of the machinery used for the addition and removal of acetyl groups on serine or threonine residues is in its infancy, the enzymes thus-far studied provide early insight into the mechanism of this newly discovered post-translational modification, and hint at its potential importance. For example, acetylation can compete with phosphorylation targeted to the same residues and could, therefore, alter the course of signaling pathways. What are the implications for signal transduction in eukaryotes and how widespread could acetylation of serine and threonine prove to be?
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U2 - 10.1016/j.tibs.2007.03.007
DO - 10.1016/j.tibs.2007.03.007
M3 - Article
C2 - 17412595
AN - SCOPUS:34247869836
SN - 0968-0004
VL - 32
SP - 210
EP - 216
JO - Trends in biochemical sciences
JF - Trends in biochemical sciences
IS - 5
ER -