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- Title
Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion.
- Authors
Veit, Michael; Laage, Rico; Dietrich, Lars; Wang, Li; Ungermann, Christian
- Abstract
Activated fatty acids stimulate budding and fusion in several cell-free assays for vesicular transport. This stimulation is thought to be due to protein palmitoylation, but relevant substrates have not yet been identified. We now report that Vac8p, a protein known to be required for vacuole inheritance, becomes patmitoylated when isolated yeast vacuoles are incubated under conditions that allow membrane fusion. Similar requirements for Vac8p patmitoylation and vacuole fusion, the inhibition of vacuole fusion by antibodies to Vac8p and the strongly reduced fusion of vacuoles tacking Vac8p suggest that patmitoylated Vac8p is essential for homotypic vacuole fusion. Strikingly, palmitoylation of Vac8p is blocked by the addition of antibodies to Secl8p (yeast NSF) only. Consistent with this, a portion of Vac8p is associated with the SNARE complex on vacuotes, which is lost during Secl8p- and ATP-dependent priming. During or after SNARE complex disassembly, palmitoylation occurs and anchors Vac8p to the vacuolar membrane. We propose that patmitoylation of Vac8p is regulated by the same machinery that controls membrane fusion.
- Subjects
PLANT vacuoles; FATTY acids; VESICULAR stomatitis; IMMUNOGLOBULINS; MEMBRANE fusion; PLANT cells &; tissues
- Publication
EMBO Journal, 2001, Vol 20, Issue 12, p3145
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1093/emboj/20.12.3145