Structure and Mechanism of DHHC Protein Acyltransferases.

Journal of Molecular Biology
Robyn StixAnirban Banerjee

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.

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Citations

Mar 4, 2021·Open Biology·Tandrila DasHoward C Hang
Apr 6, 2021·Frontiers in Molecular Biosciences·Carla Busquets-Hernández, Gemma Triola
Dec 1, 2020·Journal of Proteome Research·Yang Wang, Wei Yang
Apr 22, 2021·Open Biology·Martin Ian P Malgapo, Maurine E Linder
Aug 25, 2021·The Journal of Biological Chemistry·Robbins PuthenveetilAnirban Banerjee

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