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J. Biol. Chem., Vol. 277, Issue 31, 28271-28279, August 2, 2002
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From the The regulation of SNARE complex assembly likely
plays an important role in governing the specificity as well as the
timing of membrane fusion. Here we identify a novel brain-enriched
protein, amisyn, with a tomosyn- and VAMP-like coiled-coil-forming
domain that binds specifically to syntaxin 1a and syntaxin 4 both
in vitro and in vivo, as assessed by
co-immunoprecipitation from rat brain. Amisyn is mostly cytosolic, but
a fraction co-sediments with membranes. The amisyn coil domain can form
SNARE complexes of greater thermostability than can VAMP2 with syntaxin
1a and SNAP-25 in vitro, but it lacks a transmembrane
anchor and so cannot act as a v-SNARE in this complex. The amisyn coil
domain prevents the SNAP-25 C-terminally mediated rescue of botulinum
neurotoxin E inhibition of norepinephrine exocytosis in permeabilized
PC12 cells to a greater extent than it prevents the regular exocytosis of these vesicles. We propose that amisyn forms nonfusogenic complexes with syntaxin 1a and SNAP-25, holding them in a conformation ready for
VAMP2 to replace it to mediate the membrane fusion event, thereby
contributing to the regulation of SNARE complex formation.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF391153.
Amisyn, a Novel Syntaxin-binding Protein That May Regulate SNARE
Complex Assembly*
§,¶,
, and**
Howard Hughes Medical Institute, Department
of Molecular and Cellular Physiology, Stanford University School of
Medicine, Stanford, California 94305-5345 and Rigel,
Incorporated, South San Francisco, California 94080
*
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.
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