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	J. Cell Biol. Sep (2005); 170(7):1091-9
The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p-
Smotrys JE, Schoenfish MJ, Stutz MA, Linder ME
Department of Cell Biology and Physiology, Washington University School of Medicine, St- Louis, MO 63110, USA-
Abstract: Palmitoylation of the vacuolar membrane protein Vac8p is essential for vacuole fusion in yeast -Veit, M-, R- Laage, L- Dietrich, L- Wang, and C- Ungermann- 2001- EMBO J- 20-3145-3155; Wang, Y-X-, E-J- Kauffman, J-E- Duex, and L-S- Weisman- 2001- J- Biol- Chem- 276-35133-35140-- Proteins that contain an Asp-His-His-Cys -DHHC--cysteine rich domain -CRD- are emerging as a family of protein acyltransferases, and are therefore candidates for mediators of Vac8p palmitoylation- Here we demonstrate that the DHHC-CRD proteins Pfa3p -protein fatty acyltransferase 3, encoded by YNL326c- and Swf1p are important for vacuole fusion- Cells lacking Pfa3p had fragmented vacuoles when stressed, and cells lacking both Pfa3p and Swf1p had fragmented vacuoles under normal growth conditions- Pfa3p promoted Vac8p membrane association and palmitoylation in vivo and partially purified Pfa3p palmitoylated Vac8p in vitro, establishing Vac8p as a substrate for palmitoylation by Pfa3p- Vac8p is the first N-myristoylated, palmitoylated protein identified as a substrate for a DHHC-CRD protein-
[PUBMED: 16186255]