Premium
On the mechanism of protein palmitoylation
Author(s) -
Dietrich Lars E P,
Ungermann Christian
Publication year - 2004
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400277
Subject(s) - palmitoylation , acyltransferases , effector , prenylation , biochemistry , lipid anchored protein , ankyrin repeat , acylation , cysteine , biology , context (archaeology) , myristoylation , microbiology and biotechnology , chemistry , phosphorylation , enzyme , gene , apoptosis , paleontology , autophagy , biosynthesis , catalysis
Protein palmitoylation or, more specifically, S ‐acylation is a reversible post‐translational lipid modification. Despite the identification of several proteins that are altered in this way, our understanding of the enzymology of this process has been hampered by the lack of well‐characterized acyltransferases. We now know of three proteins in Saccharomyces cerevisiae that promote palmitoylation: effector of Ras function (Erf2), ankyrin‐repeat‐containing protein (Akr1) and the SNARE protein Ykt6. Erf2 and Akr1 are integral membrane proteins that contain a cysteine‐rich domain and an Asp‐His‐His‐Cys motif, both of which catalyse acylation at the carboxyl terminus of their target proteins. Recently, we discovered that Ykt6 mediates the amino‐terminal acylation of the fusion protein Vac8. Even though these three proteins differ in sequence, topology, size and substrate specificity, they might function in a similar manner. In this review, we discuss these observations in the context of a potential general mechanism of acylation.