| Literature DB >> 31872231 |
Niall J Fraser1, Jacqueline Howie2, Krzysztof J Wypijewski2, William Fuller2.
Abstract
The post-translational modification protein S-acylation (commonly known as palmitoylation) plays a critical role in regulating a wide range of biological processes including cell growth, cardiac contractility, synaptic plasticity, endocytosis, vesicle trafficking, membrane transport and biased-receptor signalling. As a consequence, zDHHC-protein acyl transferases (zDHHC-PATs), enzymes that catalyse the addition of fatty acid groups to specific cysteine residues on target proteins, and acyl proteins thioesterases, proteins that hydrolyse thioester linkages, are important pharmaceutical targets. At present, no therapeutic drugs have been developed that act by changing the palmitoylation status of specific target proteins. Here, we consider the role that palmitoylation plays in the development of diseases such as cancer and detail possible strategies for selectively manipulating the palmitoylation status of specific target proteins, a necessary first step towards developing clinically useful molecules for the treatment of disease.Entities:
Keywords: drug discovery and design; palmitoylation; protein S-acylation; thioesterase; zDHHC protein acyltransferase
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Year: 2020 PMID: 31872231 DOI: 10.1042/BST20190707
Source DB: PubMed Journal: Biochem Soc Trans ISSN: 0300-5127 Impact factor: 5.407