Interaction between a Ras and a Rho GTPase Couples Selection of a Growth Site to the Development of Cell Polarity in Yeast
| Autor: | Elizabeth Angerman, Charles Boone, Hay-Oak Park, Laure Béven, Keith G. Kozminski, Amy Hin Yan Tong |
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| Přispěvatelé: | Génie Enzymatique et Cellulaire (GEC), Université de Technologie de Compiègne (UTC)-Université de Picardie Jules Verne (UPJV)-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2003 |
| Předmět: |
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Molecular Saccharomyces cerevisiae Proteins Polarity (physics) Saccharomyces cerevisiae Cell Cycle Proteins CDC42 GTPase 03 medical and health sciences 0302 clinical medicine Proto-Oncogene Proteins Cell polarity Cell cortex Guanine Nucleotide Exchange Factors Cloning Molecular Molecular Biology 030304 developmental biology cdc42 GTP-Binding Protein Saccharomyces cerevisiae 0303 health sciences biology Cell Polarity Articles Cell Biology biology.organism_classification Actin cytoskeleton Protein Structure Tertiary Cell biology rab GTP-Binding Proteins Guanine nucleotide exchange factor 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Molecular Biology of the Cell Molecular Biology of the Cell, American Society for Cell Biology, 2003, 14, pp.4958-4970 Molecular Biology of the Cell, American Society for Cell Biology, 2004, 15, pp.355A |
| ISSN: | 1939-4586 1059-1524 |
| Popis: | Polarized cell growth requires the coupling of a defined spatial site on the cell cortex to the apparatus that directs the establishment of cell polarity. In the budding yeast Saccharomyces cerevisiae, the Ras-family GTPase Rsr1p/Bud1p and its regulators select the proper site for bud emergence on the cell cortex. The Rho-family GTPase Cdc42p and its associated proteins then establish an axis of polarized growth by triggering an asymmetric organization of the actin cytoskeleton and secretory apparatus at the selected bud site. We explored whether a direct linkage exists between the Rsr1p/Bud1p and Cdc42p GTPases. Here we show specific genetic interactions between RSR1/BUD1 and particular cdc42 mutants defective in polarity establishment. We also show that Cdc42p coimmunoprecipitated with Rsr1p/Bud1p from yeast extracts. In vitro studies indicated a direct interaction between Rsr1p/Bud1p and Cdc42p, which was enhanced by Cdc24p, a guanine nucleotide exchange factor for Cdc42p. Our findings suggest that Cdc42p interacts directly with Rsr1p/Bud1p in vivo, providing a novel mechanism by which direct contact between a Ras-family GTPase and a Rho-family GTPase links the selection of a growth site to polarity establishment. |
| Databáze: | OpenAIRE |
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