Seven novel mammalian SNARE proteins localize to distinct membrane compartments.
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.
Advani
R J
RJ
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University, Stanford, California 94305-5345, USA.
Bae
H R
HR
Bock
J B
JB
Chao
D S
DS
Doung
Y C
YC
Prekeris
R
R
Yoo
J S
JS
Scheller
R H
RH
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D002451:Cell Compartmentation; D002462:Cell Membrane / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D015388:Organelles / Q000378:metabolism; D051381:Rats; D050600:SNARE Proteins; D017386:Sequence Homology, Amino Acid; D033921:Vesicular Transport Proteins
D008565:Membrane Proteins; D050600:SNARE Proteins; D033921:Vesicular Transport Proteins