Methods. 2006 Oct;40(2):171-6.

Probing protein palmitoylation at the yeast vacuole.

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University of Osnabrück, Department of Biology, Barbarastrasse 13, 49076 Osnabrück, Germany.

Abstract

A protein's function depends on its localization to the right cellular compartment. A number of proteins require lipidation to associate with membranes. Protein palmitoylation is a reversible lipid modification and has been shown to mediate both membrane localization and control protein function. At the yeast vacuole, several palmitoylated proteins have been identified that are required for vacuole biogenesis, including the fusion factor Vac8, the SNARE Ykt6 and the casein kinase Yck3. Moreover, both the DHHC-CRD acyltransferase Pfa3 and Ykt6 are involved in palmitoylation at the vacuole Here, we present and discuss methods to probe for protein palmitoylation at vacuoles.

PMID:: 17012029; [PubMed - indexed for MEDLINE]

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The DHHC protein Pfa3 affects vacuole-associated palmitoylation of the fusion factor Vac8. [Proc Natl Acad Sci U S A. 2005]
The DHHC protein Pfa3 affects vacuole-associated palmitoylation of the fusion factor Vac8.
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Review On the mechanism of protein palmitoylation.
Dietrich LE, Ungermann C. EMBO Rep. 2004 Nov; 5(11):1053-7.
Review Protein lipidation. [FEBS J. 2007]
Review Protein lipidation.
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