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The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest

Abbas-Terki, Toufik
Published in FEBS letters. 2000, vol. 467, no. 1, p. 111-6
Abstract The molecular chaperone Cdc37 is thought to act in part as a targeting subunit of the heat-shock protein 90 (Hsp90) chaperone complex. We demonstrate here that Cdc37 is required for activity of the kinase Ste11 in budding yeast. A cdc37 mutant strain is defective in Ste11-mediated pheromone signaling and in accumulation and functional maturation of the constitutively active Ste11 version Ste11DeltaN. Moreover, Cdc37, Ste11DeltaN and Hsp90 coprecipitate pairwise. Thus, Hsp90 and Cdc37 may transiently associate with Ste11 to promote proper folding and/or association with additional regulatory factors. Our results establish Ste11 as the first endogenous Cdc37 client protein in yeast.
Keywords AllelesCell Cycle/drug effectsCell Cycle Proteins/chemistry/genetics/metabolismDrosophila ProteinsEnzyme Activation/drug effectsFungal Proteins/chemistry/genetics/metabolismHSP90 Heat-Shock Proteins/genetics/metabolismMAP Kinase Kinase Kinases/chemistry/genetics/metabolismMAP Kinase Signaling System/drug effectsMolecular Chaperones/chemistry/genetics/metabolismMutation/geneticsPheromones/pharmacologyPhosphorylationProtein BindingProtein Isoforms/genetics/metabolismRecombinant Fusion Proteins/chemistry/genetics/metabolismSaccharomyces cerevisiae/cytology/drug effects/enzymology/geneticsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsTemperatureTranscription Factors
PMID: 10664467
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ABBAS-TERKI, Toufik, DONZE, Olivier, PICARD, Didier. The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest. In: FEBS letters, 2000, vol. 467, n° 1, p. 111-6. doi: 10.1016/S0014-5793(00)01134-0 https://archive-ouverte.unige.ch/unige:4652

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Deposited on : 2009-12-10

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