Structure and function of DHHC protein S-acyltransferases

被引:54
作者
Gottlieb, Colin D. [1 ,2 ]
Linder, Maurine E. [1 ]
机构
[1] Cornell Univ, Coll Vet Med, Dept Mol Med, Ithaca, NY 14853 USA
[2] Stanford Univ, Dept Biol, Stanford, CA 94305 USA
关键词
CYSTEINE-RICH DOMAIN; PALMITOYL TRANSFERASE; HIPPO PATHWAY; YEAST; SUBSTRATE; MOTIF; ACID; RAS; PALMITOYLTRANSFERASE; IDENTIFICATION;
D O I
10.1042/BST20160304
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
It has been estimated that 10% of the human genome encodes proteins that are fatty acylated at cysteine residues. The vast majority of these proteins are modified by members of the DHHC protein family, which carry out their enzymatic function on the cytoplasmic face of cell membranes. The biomedical importance of DHHC proteins is underscored by their association with human disease; unique and essential roles for DHHC proteins have been uncovered using DHHC-deficient mouse models. Accordingly, there is great interest in elucidating the molecular mechanisms that underlie DHHC protein function. In this review, we present recent insights into the structure and function of DHHC enzymes.
引用
收藏
页码:923 / 928
页数:6
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