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J Biol Chem, Vol. 275, Issue 2, 1191-1200, January 14, 2000
From the Departments of Pharmacology and Physiology, Bowles Center
for Alcohol Studies, School of Medicine, University of North Carolina,
Chapel Hill, North Carolina 27599
Synaptosome-associated protein of 25 kDa
(SNAP-25) is a presynaptic membrane protein that has been clearly
implicated in membrane fusion in both developing and mature neurons,
although its mechanisms of action are unclear. We have now identified a
novel SNAP-25-interacting protein named SNIP. SNIP is a hydrophilic,
145-kDa protein that comprises two predicted coiled-coil domains, two
highly charged regions, and two proline-rich domains with multiple
PPXY and PXXP motifs. SNIP is selectively
expressed in brain where it co-distributes with SNAP-25 in most brain
regions. Biochemical studies have revealed that SNIP is tightly
associated with the brain cytoskeleton. Subcellular fractionation
and immunofluorescence localization studies have demonstrated that SNIP
co-localizes with SNAP-25 as well as the cortical actin cytoskeleton,
suggesting that SNIP serves as a linker protein connecting SNAP-25 to
the submembranous cytoskeleton. By using deletion analysis, we have
mapped the binding domains of SNIP and SNAP-25, and we have
demonstrated that the SNIP-SNAP-25 association is mediated via
coiled-coil interactions. Moreover, we have shown that overexpression
of SNIP or its SNAP-25-interacting domain inhibits
Ca2+-dependent exocytosis from PC12 cells.
These results indicate that SNIP is involved in regulation of
neurosecretion, perhaps via its interaction with SNAP-25 and the cytoskeleton.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF156981 and AF156982.
SNIP, a Novel SNAP-25-interacting Protein Implicated in
Regulated Exocytosis*
*
This work was supported by National Institutes of Health
Grant NS37939, University of North Carolina Junior Faculty Development award, and grants from the University of North Carolina Research Council and the Foundation of Hope (to L. L.).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.
To whom correspondence should be addressed: Dept. of Pharmacology,
Rm. 1025A Thurston-Bowles, University of North Carolina, Chapel Hill,
NC 27599-7178. Tel.: 919-966-0503; Fax: 919-966-5679; E-mail:
LianLi@med.unc.edu.
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