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Literature DB >> 8641455

Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25.

Abstract

Synaptotagmin, a likely calcium sensor for synaptic transmission, and SNAP-25, a t-SNARE of the presynaptic plasma membrane, are key proteins for the docking and fusion of synaptic and other vesicles. We report that both synaptotagmin and SNAP-25 are palmitoylated with their fatty acids attached in a labile thioester-type bond. A SNAP-25 mutant with deleted palmitoylation sites is found exclusively in the cytosol after cell fractionation, whereas the palmitoylated form of SNAP-25 is membrane-bound, establishing that SNAP-25 is membrane-anchored via covalently linked palmitate.

Entities: Chemical Gene

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Year: 1996 PMID： 8641455 DOI： 10.1016/0014-5793(96)00362-6

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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Cited

69 in total

1. Phosphorylation of SNAP-23 by the novel kinase SNAK regulates t-SNARE complex assembly.

Authors: J P Cabaniols; V Ravichandran; P A Roche
Journal: Mol Biol Cell Date: 1999-12 Impact factor: 4.138

2. Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation.

Authors: Masayoshi Fukasawa; Oleg Varlamov; William S Eng; Thomas H Söllner; James E Rothman
Journal: Proc Natl Acad Sci U S A Date: 2004-03-24 Impact factor: 11.205

3. Chemomechanical regulation of SNARE proteins studied with molecular dynamics simulations.

Authors: Lars V Bock; Brian Hutchings; Helmut Grubmüller; Dixon J Woodbury
Journal: Biophys J Date: 2010-08-09 Impact factor: 4.033

4. Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation.

Authors: Javier Valdez-Taubas; Hugh Pelham
Journal: EMBO J Date: 2005-06-23 Impact factor: 11.598

Review 5. The t-SNARE complex: a close up.

Authors: Alison R Dun; Colin Rickman; Rory R Duncan
Journal: Cell Mol Neurobiol Date: 2010-11-03 Impact factor: 5.046

Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25.

1. Phosphorylation of SNAP-23 by the novel kinase SNAK regulates t-SNARE complex assembly.

2. Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation.

3. Chemomechanical regulation of SNARE proteins studied with molecular dynamics simulations.

4. Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation.

Review 5. The t-SNARE complex: a close up.

6. Differential palmitoylation regulates intracellular patterning of SNAP25.

7. SNAP25 expression in mammalian retinal horizontal cells.

8. Association of botulinum neurotoxin serotype A light chain with plasma membrane-bound SNAP-25.

9. Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion.

10. Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8.