SNAP-23 and SNAP-25 Are Palmitoylated in Vivo

Author: Vogel K.   Roche P.A.  

Publisher: Elsevier

ISSN: 0006-291X

Source: Biochemical and Biophysical Research Communications, Vol.258, Iss.2, 1999-05, pp. : 407-410

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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.