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EMBO reports 5, 11, 1053–1057 (2004)
doi:10.1038/sj.embor.7400277
On the mechanism of protein palmitoylation
Lars E.P. Dietrich & Christian Ungermann
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Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany
To whom correspondence should be addressed
Christian Ungermann Tel: +49 6221 544 180; Fax: +49 6221 544 366; cu2@ix.urz.uni-heidelberg.de
Received 9 July 2004; Accepted 26 August 2004.
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Abstract
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.
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