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FEBS Lett. 1996 Apr 29;385(1-2):119-23.

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

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1
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, 10021, USA.

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.

PMID:
8641455
DOI:
10.1016/0014-5793(96)00362-6
[Indexed for MEDLINE]
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