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First published online 25 August 2004
doi: 10.1242/jcs.01349

Journal of Cell Science 117, 4757-4767 (2004)
Published by The Company of Biologists 2004
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Research Article

Gyp5p and Gyl1p are involved in the control of polarized exocytosis in budding yeast

Laurent Chesneau1,*, Sophie Dupré1,*, Anna Burdina1, Jérôme Roger1,{ddagger}, Sophie Le Panse2, Michel Jacquet1 and Marie-Hélène Cuif1,¶

1 Institut de Génétique et Microbiologie, CNRS-UMR 8621, Université Paris XI, 91 405 Orsay Cédex, France
2 Service de Microscopie Electronique, Institut J. Monod, 75251 Paris CEDEX 05, France

Author for correspondence (e-mail: mhcuif{at}igmors.u-psud.fr)

Accepted 7 June 2004

We report here elements for functional characterization of two members of the Saccharomyces cerevisiae Ypt/Rab GTPase activating proteins family (GAP): Gyp5p, a potent GAP in vitro for Ypt1p and Sec4p, and the protein Ymr192wp/APP2 that we propose to rename Gyl1p (GYp like protein). Immunofluorescence experiments showed that Gyp5p and Gyl1p partly colocalize at the bud emergence site, at the bud tip and at the bud neck during cytokinesis. Subcellular fractionation and co-immunoprecipitation experiments showed that Gyp5p and Gyl1p co-fractionate with post-Golgi vesicles and plasma membrane, and belong to the same protein complexes in both localizations. We found by co-immunoprecipitation experiments that a fraction of Gyp5p interacts with Sec4p, a small GTPase involved in exocytosis, and that a fraction of Gyl1p associates at the plasma membrane with the Gyp5p/Sec4p complexes. We showed also that GYP5 genetically interacts with SEC2, which encodes the Sec4p exchange factor. Examination of the gyp5{Delta}gyl1{Delta} mutants grown at 13°C revealed a slight growth defect, a secretion defect and an accumulation of secretory vesicles in the small-budded cells. These data suggest that Gyp5p and Gyl1p are involved in control of polarized exocytosis.

Key words: Gyp5p, Ymr192wp, Sec4p, Polarized exocytosis




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