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Trends Biochem Sci. 2017 Jul;42(7):566-581. doi: 10.1016/j.tibs.2017.04.004. Epub 2017 Jun 8.

Dynamic Protein Acylation: New Substrates, Mechanisms, and Drug Targets.

Author information

1
Institute of Chemical Biology, Department of Chemistry, Imperial College London, London SW7 2AZ, UK.
2
Institute of Chemical Biology, Department of Chemistry, Imperial College London, London SW7 2AZ, UK. Electronic address: e.tate@imperial.ac.uk.

Abstract

Post-translational attachment of lipids to proteins is found in all organisms, and is important for many biological processes. Acylation with myristic and palmitic acids are among the most common lipid modifications, and understanding reversible protein palmitoylation dynamics has become a particularly important goal. Linking acyltransferase enzymes to disease states can be challenging due to a paucity of robust models, compounded by functional redundancy between many palmitoyl transferases; however, in cases such as Wnt or Hedgehog signalling, small molecule inhibitors have been identified, with some progressing to clinical trials. In this review, we present recent developments in our understanding of protein acylation in human health and disease through use of chemical tools, global profiling of acylated proteomes, and functional studies of specific protein targets.

KEYWORDS:

chemical biology; myristoylation; palmitoylation; post-translational modification; proteomics

PMID:
28602500
DOI:
10.1016/j.tibs.2017.04.004
[Indexed for MEDLINE]
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