Article
- The EMBO Journal (2003) 23, 45 - 53
- doi:10.1038/sj.emboj.7600015
Published online: 11 December 2003
Subject Categories:
The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion
Lars EP Dietrich1, Rolf Gurezka1,3, Michael Veit2 and Christian Ungermann1
- Biochemie-Zentrum Heidelberg (BZH), University of Heidelberg, Heidelberg, Germany
- Department of Immunology and Molecular Biology, Vet.-Med. Faculty of the Free University Berlin, Berlin, Germany
- Current address: BioReliance Manufacturing GmbH, Cernyring 22, 69115 Heidelberg, Germany
Correspondence to:
Christian Ungermann, Biochemie-Zentrum Heidelberg (BZH), University of Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany. Tel.: +49 6221 544180; Fax: +49 6221 544366; E-mail: cu2@ix.urz.uni-heidelberg.de
Received 25 August 2003; Accepted 17 October 2003
Abstract
The NSF homolog Sec18 initiates fusion of yeast vacuoles by disassembling cis-SNARE complexes during priming. Sec18 is also required for palmitoylation of the fusion factor Vac8, although the acylation machinery has not been identified. Here we show that the SNARE Ykt6 mediates Vac8 palmitoylation and acts during a novel subreaction of vacuole fusion. This subreaction is controlled by a Sec17-independent function of Sec18. Our data indicate that Ykt6 presents Pal-CoA via its N-terminal longin domain to Vac8, while transfer to Vac8's SH4 domain occurs spontaneously and not enzymatically. The conservation of Ykt6 and its localization to several organelles suggest that its acyltransferase activity may also be required in other intracellular fusion events.
Keywords:
- palmitoylation,
- Sec18,
- vacuole fusion,
- Ykt6,
- SNARE
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