出版社：American Society for Biochemistry and Molecular Biology
摘要：Protein palmitoylation refers to the posttranslational additionof a 16 carbon fatty acid to the side chain of cysteine, forminga thioester linkage. This acyl modification is readily reversible,providing a potential regulatory mechanism to mediate protein-membraneinteractions and subcellular trafficking of proteins. The mechanismthat underlies the transfer of palmitate or other long-chainfatty acids to protein was uncovered through genetic screensin yeast. Two related S-palmitoyltransferases were discovered.Erf2 palmitoylates yeast Ras proteins, whereas Akr1 modifiesthe yeast casein kinase, Yck2. Erf2 and Akr1 share a commonsequence referred to as a DHHC (aspartate-histidine-histidine-cysteine)domain. Numerous genes encoding DHHC domain proteins are foundin all eukaryotic genome databases. Mounting evidence is consistentwith this signature motif playing a direct role in protein acyltransferase(PAT) reactions, although many questions remain. This reviewpresents the genetic and biochemical evidence for the PAT activityof DHHC proteins and discusses the mechanism of protein-mediatedpalmitoylation.Supplementary key words fatty acylation • cysteine rich domain • palmitoyl-CoenzymeA
