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The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest
T Abbas-Terki1, O Donzé, D Picard
1Département de Biologie Cellulaire, Université de Genève, Sciences III, 30 quai Ernest-Ansermet, CH-1211, Genève, Switzerland.
FEBS Letters
|February 9, 2000
Summary
The molecular chaperone Cdc37 is essential for the activity of the Ste11 kinase in yeast. This study identifies Ste11 as the first endogenous Cdc37 client protein, revealing new insights into chaperone function.
Area of Science:
- Molecular biology
- Cellular signaling
- Protein biochemistry
Background:
- The molecular chaperone Cdc37 (cell division cycle 37) is implicated as a targeting subunit of the heat-shock protein 90 (Hsp90) chaperone complex.
- The precise endogenous client proteins of Cdc37 in yeast have not been definitively identified.
Purpose of the Study:
- To investigate the role of Cdc37 in the activity of the Ste11 kinase in budding yeast.
- To identify Ste11 as a potential endogenous client protein of Cdc37.
Main Methods:
- Genetic analysis of a cdc37 mutant strain in budding yeast.
- Assessment of Ste11-mediated pheromone signaling pathways.
- Analysis of Ste11 protein accumulation and functional maturation.
- Coprecipitation assays to detect protein-protein interactions between Cdc37, Hsp90, and Ste11.
Main Results:
- A cdc37 mutant strain exhibited defects in Ste11-mediated pheromone signaling.
- The mutant strain showed impaired accumulation and functional maturation of a constitutively active Ste11 variant (Ste11DeltaN).
- Cdc37, Hsp90, and Ste11DeltaN were found to coprecipitate, indicating pairwise associations.
Conclusions:
- Cdc37 is required for the activity of the Ste11 kinase in budding yeast.
- Hsp90 and Cdc37 likely associate transiently with Ste11 to facilitate proper protein folding and/or interaction with regulatory factors.
- Ste11 is established as the first identified endogenous Cdc37 client protein in yeast.