Abstract
Acetylation of the epsilon-amino group of lysine residues, or N(epsilon)-lysine acetylation, is an important post-translational modification known to occur in histones, transcription factors and other proteins. Since 1995, dozens of proteins have been discovered to possess intrinsic lysine acetyltransferase activity. Although most of these enzymes were first identified as histone acetyltransferases and then tested for activities towards other proteins, acetyltransferases only modifying non-histone proteins have also been identified. Lysine acetyltransferases form different groups, three of which are Gcn5/PCAF, p300/CBP and MYST proteins. While members of the former two groups mainly function as transcriptional co-activators, emerging evidence suggests that MYST proteins, such as Esa1, Sas2, MOF, TIP60, MOZ and MORF, have diverse roles in various nuclear processes. Aberrant lysine acetylation has been implicated in oncogenesis. The genes for p300, CBP, MOZ and MORF are rearranged in recurrent leukemia-associated chromosomal abnormalities. Consistent with their roles in leukemogenesis, these acetyltransferases interact with Runx1 (or AML1), one of the most frequent targets of chromosomal translocations in leukemia. Therefore, the diverse superfamily of lysine acetyltransferases executes an acetylation program that is important for different cellular processes and perturbation of such a program may cause the development of cancer and other diseases.
Highlights
The question of how protein functions are regulated in vivo has been and remains a central issue in studies of various biological processes
This type of modi®cation ought to be distinguished from acetylation of the a-amino groups of N-terminal residues, or Na-terminal acetylation, which occurs in many eukaryotic proteins [12]
Evidence for the involvement of aberrant histone acetyltransferase (HAT) in human leukemia will be described at the end, to conclude that LATs are potential molecular targets for therapeutic intervention of leukemia and other diseases caused by abnormal lysine acetylation
Summary
The question of how protein functions are regulated in vivo has been and remains a central issue in studies of various biological processes. I will discuss how activities of LATs are regulated, what determines their substrate speci®city and how lysine acetylation affects protein function.
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