Sec1p Binds to SNARE Complexes and Concentrates at Sites of Secretion

doi:10.1083/jcb.146.2.333

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J. Cell Biol., Volume 146, Number 2, July 26, 1999 333-344
Copyright © 1999 by The Rockefeller University Press.

Sec1p Binds to SNARE Complexes and Concentrates at Sites of Secretion

Chavela M. Carr^a, Eric Grote^a, Mary Munson^b, Frederick M. Hughson^b, and Peter J. Novick^a
^a Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510
^b Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544

Correspondence to: Peter J. Novick, Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510., peter.novick{at}yale.edu (E-mail), (203) 785-5871 (phone), (203) 785-7226 (fax)

Proteins of the Sec1 family have been shown to interact withtarget-membrane t-SNAREs that are homologous to the neuronalprotein syntaxin. We demonstrate that yeast Sec1p coprecipitatesnot only the syntaxin homologue Ssop, but also the other twoexocytic SNAREs (Sec9p and Sncp) in amounts and in proportionscharacteristic of SNARE complexes in yeast lysates. The interactionbetween Sec1p and Ssop is limited by the abundance of SNAREcomplexes present in sec mutants that are defective in eitherSNARE complex assembly or disassembly. Furthermore, the localizationof green fluorescent protein (GFP)-tagged Sec1p coincides withsites of vesicle docking and fusion where SNARE complexes arebelieved to assemble and function. The proposal that SNARE complexesact as receptors for Sec1p is supported by the mislocalizationof GFP-Sec1p in a mutant defective for SNARE complex assemblyand by the robust localization of GFP-Sec1p in a mutant thatfails to disassemble SNARE complexes. The results presentedhere place yeast Sec1p at the core of the exocytic fusion machinery,bound to SNARE complexes and localized to sites of secretion.

Key Words: Sec1 proteins, syntaxin proteins, SNARE complex, secretion,yeast

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