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Biochem Biophys Res Commun. 1999 May 10;258(2):407-10.

SNAP-23 and SNAP-25 are palmitoylated in vivo.

Author information

1
Experimental Immunology Branch, National Cancer Institute, Bethesda, Maryland 20892, USA.

Abstract

The neuronal presynaptic membrane t-SNARE complex consists of the transmembrane protein syntaxin with the palmitoylated protein SNAP-25. In non-neuronal tissues, SNAP-23 replaces SNAP-25 in the t-SNARE complex, although the mechanism of membrane anchoring of SNAP-23 has not been determined. We now report that like SNAP-25, SNAP-23 is palmitoylated in vivo on one or more cysteine residues present in a central "palmitoylation domain." Interestingly, SNAP-23 is palmitoylated less well than SNAP-25, and in vivo binding studies indicate a correlation between the extent of palmitoylation and the ability of SNAP-23 or SNAP-25 to bind to syntaxin in vivo.

PMID:
10329400
DOI:
10.1006/bbrc.1999.0652
[Indexed for MEDLINE]

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