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J Biol Chem, Vol. 273, Issue 17, 10317-10324, April 24, 1998
From the Howard Hughes Medical Institute, Department of Molecular
and Cellular Physiology, Stanford University,
Stanford, California 94305-5345
Soluble
N-ethylmaleimide-sensitive factor-attachment protein
receptor (SNARE) proteins of the vesicle-associated membrane protein
(VAMP) and syntaxin families play a central role in vesicular trafficking through the formation of complexes between proteins present
on vesicle and target membranes. Formation of these complexes is
proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. In order to further understand the molecular mechanisms that organize membrane
compartments, we have characterized seven new mammalian proteins of the
VAMP and syntaxin families. The proteins are broadly expressed;
however, syntaxin 13 is enriched in brain and VAMP 8 in kidney. The
seven novel SNAREs localize in distinct patterns overlapping with
Golgi, endosomal, or lysosomal markers. Our studies support the
hypothesis that evolutionary radiation of these two gene families gave
rise to sets of proteins whose differential expression and
combinatorial associations define and organize the membrane
compartments of cells.
Seven Novel Mammalian SNARE Proteins Localize to Distinct
Membrane Compartments
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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