The RabGAP Proteins Gyp5p and Gyl1p Recruit the BAR Domain Protein Rvs167p for Polarized Exocytosis

The Rab GTPase‐activating proteins (GAP) Gyp5p and Gyl1p are involved in the control of polarized exocytosis at the small‐bud stage in Saccharomyces cerevisiae. Both Gyp5p and Gyl1p interact with the N‐Bin1/Amphiphysin/Rvs167 (BAR) domain protein Rvs167p, but the biological function of this interact...

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Veröffentlicht in:	Traffic (Copenhagen, Denmark) Denmark), 2011-08, Vol.12 (8), p.1084-1097
Hauptverfasser:	Prigent, Magali, Boy‐Marcotte, Emmanuelle, Chesneau, Laurent, Gibson, Kimberley, Dupré‐Crochet, Sophie, Tisserand, Hélène, Verbavatz, Jean‐Marc, Cuif, Marie‐Hélène
Format:	Artikel
Sprache:	eng
Schlagworte:	Exocytosis - genetics Exocytosis - physiology Glucan Endo-1,3-beta-D-Glucosidase - metabolism GTPase-Activating Proteins - genetics GTPase-Activating Proteins - metabolism Gyl1p Gyp5p Microfilament Proteins - genetics Microfilament Proteins - metabolism Mutation Nerve Tissue Proteins - metabolism N‐BAR domain polarized exocytosis Proline - genetics Proline - metabolism Protein Binding Protein Interaction Domains and Motifs rab GTP-Binding Proteins - genetics rab GTP-Binding Proteins - metabolism RabGAP Rvs167p Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Secretory Vesicles - metabolism src Homology Domains
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