ArticleThe Biochemical journal2000
Palmitoylation of the 25-kDa synaptosomal protein (SNAP-25) in vitro occurs in the absence of an enzyme, but is stimulated by binding to syntaxin.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 65 citations in OpenAlex.
- Palmitoyltransferase DHHC13 controls lysosomal cholesterol egress through palmitoylating Niemann-Pick C1.Life metabolism · 2026Article
- Multiple structural states in an intrinsically disordered protein, SNAP-25, using circular dichroism.Biophysical journal · 2025Article
- Lipids and Secretory Vesicle Exocytosis.Advances in neurobiology · 2023Article
- Protein palmitoylation: Palmitoyltransferases and their specificity.Experimental biology and medicine (Maywood, N.J.) · 2017Article
- Roles of cysteine residues in the inhibition of human glutamate dehydrogenase by palmitoyl-CoA.BMB reports · 2012Article
- Palmitoylation of virus proteins.Biology of the cell · 2012Review
- SNAP25 expression in mammalian retinal horizontal cells.The Journal of comparative neurology · 2011Article
- Proteomic analysis of fatty-acylated proteins in mammalian cells with chemical reporters reveals S-acylation of histone H3 variants.Molecular & cellular proteomics : MCP · 2011Article
- Characterization of the self-palmitoylation activity of the transport protein particle component Bet3.Cellular and molecular life sciences : CMLS · 2010Article
- Identification of palmitoylated mitochondrial proteins using a bio-orthogonal azido-palmitate analogue.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2008Article
- Dual lipid modification of Arabidopsis Ggamma-subunits is required for efficient plasma membrane targeting.Plant physiology · 2007Article
- Unique self-palmitoylation activity of the transport protein particle component Bet3: a mechanism required for protein stability.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Article
- Promiscuous interaction of SNAP-25 with all plasma membrane syntaxins in a neuroendocrine cell.The Biochemical journal · 2005Article
- The human SNARE protein Ykt6 mediates its own palmitoylation at C-terminal cysteine residues.The Biochemical journal · 2004Article
- On the mechanism of protein palmitoylation.EMBO reports · 2004Review
- The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion.The EMBO journal · 2004Article
- A cell-specific, prenylation-independent mechanism regulates targeting of type II RACs.The Plant cell · 2002Article
- Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting.The Biochemical journal · 2001Article
- Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion.The EMBO journal · 2001Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The neuronal N-ethylmaleimide-sensitive-factor-attachment-protein receptor (SNARE) proteins 25-kDa synaptosomal protein (SNAP-25), syntaxin 1 and synaptobrevin 2 interact to form the intermembrane SNARE complex, which mediates docking and fusion of synaptic vesicles with the plasma membrane. Assembly of the SNARE complex is accompanied by conformational changes, especially in SNAP-25. SNAP-25 is palmitoylated in vivo at cysteine residues located in the middle of the molecule. Acylation is required for membrane binding or membrane targeting of this intrinsically hydrophilic protein. Palmitoylation of recombinant SNAP-25 was studied in vitro in the absence of an enzyme source with [(3)H]palmitoyl-CoA as the lipid donor. [(3)H]Palmitate incorporation into unbound SNAP-25 was negligible, but was stimulated 100-fold when SNAP-25 was present in the SNARE complex. SNAP-25 in a binary complex with syntaxin 1 was palmitoylated with almost the same efficiency. A mutant of SNAP-25, which was not acylated in vivo, did not incorporate [(3)H]palmitate in this assay. [(3)H]Palmitate incorporation into wild-type SNAP-25 was blocked by chemical blocking of free SH groups, but slightly stimulated by reduction of disulfide-bonds. This shows that palmitoylation of SNAP-25 in vitro occurs at the same cysteine residues that are palmitoylated in vivo. This demonstrates that efficient palmitoylation of SNAP-25 depends on an interaction with a physiological binding partner. It suggests further that palmitoylation of SNAP-25 requires the alpha-helical conformation of the protein, which is induced by binding to syntaxin 1.
Indexed as
Identifiers
10600650PMC1220741W2009944214What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.