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Structure and Mechanism of DHHC Protein Acyltransferases.

ABSTRACT: S-acylation, whereby a fatty acid chain is covalently linked to a cysteine residue by a thioester linkage, is the most prevalent kind of lipid modification of proteins. Thousands of proteins are targets of this post-translational modification, which is catalyzed by a family of eukaryotic integral membrane enzymes known as DHHC protein acyltransferases (DHHC-PATs). Our knowledge of the repertoire of S-acylated proteins has been rapidly expanding owing to development of the chemoproteomic techniques. There has also been an increasing number of reports in the literature documenting the importance of S-acylation in human physiology and disease. Recently, the first atomic structures of two different DHHC-PATs were determined using X-ray crystallography. This review will focus on the insights gained into the molecular mechanism of DHHC-PATs from these structures and highlight representative data from the biochemical literature that they help explain.

SUBMITTER: Stix R

PROVIDER: S-EPMC7483407 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature

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Structure and Mechanism of DHHC Protein Acyltransferases.

Stix Robyn R Lee Chul-Jin CJ Faraldo-Gómez José D JD Banerjee Anirban A

Journal of molecular biology 20200606 18

S-acylation, whereby a fatty acid chain is covalently linked to a cysteine residue by a thioester linkage, is the most prevalent kind of lipid modification of proteins. Thousands of proteins are targets of this post-translational modification, which is catalyzed by a family of eukaryotic integral membrane enzymes known as DHHC protein acyltransferases (DHHC-PATs). Our knowledge of the repertoire of S-acylated proteins has been rapidly expanding owing to development of the chemoproteomic techniqu ...[more]

PMID: 32522557

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