Abstract
Protein acetylation is a well-studied
regulatory mechanism for several cellular processes, ranging from gene
expression to
metabolism. Recent discoveries of new
post-translational modifications, including malonylation, succinylation,
and glutarylation,
have expanded our understanding of the types of
modifications found on proteins. These three acidic lysine modifications
are
structurally similar but have the potential to
regulate different proteins in different pathways.
The deacylase sirtuin
5
(SIRT5) catalyzes the removal of these
modifications from a wide range of proteins in different subcellular
compartments.
Here, we review these new modifications, their
regulation by SIRT5, and their emerging role in cellular regulation and
diseases.
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