QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

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

This Article Figures Only Full Text Full Text (PDF) All Versions of this Article: jcs.01349v1 117/20/4757    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Chesneau, L. Articles by Cuif, M.-H. Search for Related Content PubMed PubMed Citation Articles by Chesneau, L. Articles by Cuif, M.-H. Social Bookmarking                         What's this?

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

Laurent Chesneau^1,*, Sophie Dupré^1,*, Anna Burdina¹, Jérôme Roger^1,, Sophie Le Panse², Michel Jacquet¹ and Marie-Hélène Cuif^1,¶

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 gyp5gyl1 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

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				G. Ren, P. Vajjhala, J. S. Lee, B. Winsor, and A. L. Munn The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy Microbiol. Mol. Biol. Rev., March 1, 2006; 70(1): 37 - 120. [Abstract] [Full Text] [PDF]

				H. Friesen, C. Humphries, Y. Ho, O. Schub, K. Colwill, and B. Andrews Characterization of the Yeast Amphiphysins Rvs161p and Rvs167p Reveals Roles for the Rvs Heterodimer In Vivo Mol. Biol. Cell, March 1, 2006; 17(3): 1306 - 1321. [Abstract] [Full Text] [PDF]

				H. Friesen, K. Colwill, K. Robertson, O. Schub, and B. Andrews Interaction of the Saccharomyces cerevisiae Cortical Actin Patch Protein Rvs167p With Proteins Involved in ER to Golgi Vesicle Trafficking Genetics, June 1, 2005; 170(2): 555 - 568. [Abstract] [Full Text] [PDF]