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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Vogel K,Roche PA

doi

10.1006/bbrc.1999.0652

subject

Has Abstract

pub_date

1999-05-10 00:00:00

pages

407-10

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(99)90652-6

journal_volume

258

pub_type

杂志文章

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