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A more recent version of this article appeared on January 1, 2004
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Submitted on July 26, 2003
Revised on September 8, 2003
Accepted on September 16, 2003
1 University of Michigan; Department of Molecular, Cellular and Developmental Biology, 830 N. University AVE, Ann Arbor, MI 48109-1048
* Corresponding author. E-mail address: jessehay{at}umich.edu.
Although some of the principles of SNAP receptor (SNARE) function are well understood, remarkably little detail is known about sec1/munc18 (SM) protein function and its relationship to SNAREs. Popular models of SM protein function hold that these proteins promote or maintain an open and/or monomeric pool of syntaxin molecules available for SNARE complex formation. To address the functional relationship of the mammalian ER/Golgi SM protein rsly1 and its SNARE binding partner syntaxin 5, we produced a conformation-specific mAb that binds only the available, but not the cis-SNARE complexed nor intramolecularly closed form of syntaxin 5. Immunostaining experiments demonstrated that syntaxin 5 SNARE motif availability is nonuniformly distributed and focally regulated. In vitro ER to Golgi transport assays revealed that rsly1 was acutely required for transport, and that binding to syntaxin 5 was absolutely required for its function. Finally, manipulation of rsly1-syntaxin 5 interactions in vivo revealed that they had remarkably little impact on the pool of available syntaxin 5 SNARE motif. Our results argue that although rsly1 does not appear to regulate the availability of syntaxin 5, its function is intimately associated with syntaxin binding, perhaps promoting a later step in SNARE complex formation or function.
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