期刊
JOURNAL OF CELL SCIENCE
卷 117, 期 4, 页码 521-526出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.00989
关键词
palmitate; protein acyltransferase; PATs; signaling
类别
资金
- NCI NIH HHS [R01 CA050211, CA50211, R01 CA050211-15A2] Funding Source: Medline
- NIGMS NIH HHS [GM51466] Funding Source: Medline
The acylation of proteins with palmitate and related fatty acids has been known for over 30 years, but the molecular machinery that carries out palmitoylation has only recently emerged from studies in. the model organisms Saccharomyces cerevisiae and Drosophila. Two classes of protein acyltransferases (PATs) have been proposed. In yeast, members of a family of integral membrane proteins harboring a cysteine-rich domain (CRD) containing a conserved DHHC (Asp-His-His-Cys) motif are PATs for cytoplasmic signaling molecules. The DHHC-CRD protein Erf2p, together with an associated subunit Erf4p, palmitoylates yeast Ras proteins, and Akr1p catalyzes the palmitoylation of the yeast casein kinase Yck2p. The existence of a second class of PATs that modify secreted signaling proteins has been suggested from work in Drosophila. Rasp is required in vivo for the production of functional Hedgehog and shares sequence identity with membrane-bound O-acyltransferases, which suggests that it catalyzes the palmitoylation of Hedgehog. With the identification of PATs in model genetic organisms, the field is now poised to uncover their mammalian counterparts and to understand the enzymology of protein palmitoylation.
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