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Vol. 12, Issue 3, 521-538, March 2001
Department of Biology, The Hong Kong University of Science and
Technology, Clearwater Bay, Kowloon, Hong Kong, China
Sed5p is the only syntaxin family member required for protein
transport through the yeast Golgi and it is known to bind up to nine
other soluble N-ethylmaleimide-sensitive factor
attachment receptor (SNARE) proteins in vivo. We describe in vitro
binding experiments in which we identify ternary and quaternary
Sed5p-containing SNARE complexes. The formation of SNARE complexes
among these endoplasmic reticulum- and Golgi-localized proteins
requires Sed5p and is syntaxin-selective. In addition, Sed5p-containing
SNARE complexes form selectively and this selectivity is mediated by Sed5p-containing intermediates that discriminate among subsequent binding partners. Although many of these SNAREs have overlapping distributions in vivo, the SNAREs that form complexes with Sed5p in
vitro reflect their functionally distinct locales. Although SNARE-SNARE interactions are promiscuous and a single SNARE protein is
often found in more than one complex, both the biochemical as well as
genetic analyses reported here suggest that this is not a result of
nonselective direct substitution of one SNARE for another. Rather our
data are consistent with the existence of multiple (perhaps parallel)
trafficking pathways where Sed5p-containing SNARE complexes play
overlapping and/or distinct functional roles.
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