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J Biol Chem, Vol. 273, Issue 51, 34171-34179, December 18, 1998
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From ¶ Rigel Inc., Sunnyvale, California 94086 and the
Intracellular membrane traffic is thought to be
regulated in part by soluble N-ethylmaleimide-sensitive
factor-attachment protein receptors (SNAREs) through the formation of
complexes between these proteins present on vesicle and target
membranes. All known SNARE-mediated fusion events involve members of
the syntaxin and vesicle-associated membrane protein families. The diversity of mammalian membrane compartments predicts the existence of
a large number of different syntaxin and vesicle-associated membrane
protein genes. To further investigate the spectrum of SNAREs and their
roles in membrane trafficking we characterized three novel members of
the syntaxin and SNAP-25 (synaptosome-associated protein of 25 kDa)
subfamilies. The proteins are broadly expressed, suggesting a general
role in vesicle trafficking, and localize to distinct membrane
compartments. Syntaxin 8 co-localizes with markers of the endoplasmic
reticulum. Syntaxin 17, a divergent member of the syntaxin family,
partially overlaps with endoplasmic reticulum markers, and SNAP-29 is
broadly localized on multiple membranes. SNAP-29 does not contain a
predicted membrane anchor characteristic of other SNAREs. In
vitro studies established that SNAP-29 is capable of binding to a
broad range of syntaxins.
Department of Molecular and Cellular Physiology, Howard
Hughes Medical Institute, Stanford University School of Medicine,
Stanford, California 94305-5345
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