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

FEBS Letters

Picard, Didier¹  Donzé, Olivier¹  Abbas-Terki, Toufik¹ 

[1] Département de Biologie Cellulaire, Université de Genève, Sciences III, 30 quai Ernest-Ansermet, CH-1211 Genève 4, Switzerland

关键词: Molecular chaperone;    Pheromone signaling;    Ste11;    Cdc37;    Hsp90;    Saccharomyces cerevisiae;    Cdc;    cell cycle division;    GST;    glutathione-S-transferase;    Hsp90;    heat-shock protein 90;    MAPK;    mitogen-activated protein kinase;   

DOI  :  10.1016/S0014-5793(00)01134-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Ste11ΔN. Moreover, Cdc37, Ste11ΔN 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.

【 授权许可】

Unknown