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J Biol Chem, Vol. 275, Issue 4, 2959-2965, January 28, 2000
From the Experimental Immunology Branch, NCI, National Institutes
of Health, Bethesda, Maryland 20892
The docking and fusion of synaptic vesicles with
the presynaptic plasma membrane require the interaction of the
vesicle-associated membrane protein VAMP with the plasma membrane
proteins syntaxin and SNAP-25. Both of these proteins behave as
integral membrane proteins, although they are unusual in that they
insert into membranes post-translationally. Whereas VAMP and syntaxin
possess hydrophobic transmembrane domains, SNAP-25 does not, and it is
widely believed that SNAP-25 traffics to and inserts into membranes by
post-translational palmitoylation. In pulse-chase biosynthesis studies,
we now show that SNAP-25 and syntaxin rapidly bind to each other while
still in the cytosol of neuroendocrine and transfected heterologous cells. Cell fractionation studies revealed that cytosolic
SNAP-25·syntaxin complexes then traffic to and insert into
membranes. Furthermore, the association of SNAP-25 with membranes
is dramatically enhanced by syntaxin, and the transmembrane domain of
syntaxin is essential for this effect. Surprisingly, despite the
importance of the SNAP-25 palmitoylation domain for membrane anchoring
at steady state, removal of this domain did not inhibit the initial
association of newly synthesized SNAP-25 with membranes in the presence
of syntaxin. These data demonstrate that the initial attachment of newly synthesized SNAP-25 to membranes is a consequence of its association with syntaxin and that it is only after syntaxin-mediated membrane tethering that SNAP-25 is palmitoylated.
Targeting of SNAP-25 to Membranes Is Mediated by Its
Association with the Target SNARE Syntaxin*
,§, and
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
These authors contributed equally to this work.
§
Present address: Inst. Pasteur, U277, Biologie Moleculaire du Gen,
25 rue du Dr. Roux, 75724 Paris Cedex 15, France.
¶
To whom correspondence should be addressed: NCI, NIH, Bldg.
10, Rm. 4B36, Bethesda, MD 20892. Tel.: 301-594-2595; Fax:
301-496-0887; E-mail: paul.roche@nih.gov.
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