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Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510
The small GTPase Sec4p is required for vesicular transport at the post-Golgi stage of yeast secretion. Here we present evidence that mutations in SEC2,
itself an essential gene that acts at the same stage of the
secretory pathway, cause Sec4p to mislocalize as a result of a random rather than a polarized accumulation
of vesicles. Sec2p and Sec4p interact directly, with the
nucleotide-free conformation of Sec4p being the preferred state for interaction with Sec2p. Sec2p functions
as an exchange protein, catalyzing the dissociation of
GDP from Sec4 and promoting the binding of GTP. We
propose that Sec2p functions to couple the activation of
Sec4p to the polarized delivery of vesicles to the site of exocytosis.
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