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Dissecting the Cdc37 cochaperone code: Functional roles in chaperone-mediated stress adaptation.

Megan M Mitchem1, Ashley Choi1, Duhita A Mirikar1

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Phosphorylation of Cdc37, a protein kinase co-chaperone, is crucial for cellular stress tolerance. This study reveals 34 new phosphorylation sites that modulate Cdc37 function in a context-dependent manner, impacting proteostasis.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Cdc37 is a crucial co-chaperone that links protein kinases to the Hsp90 chaperone machinery.
  • Phosphorylation at Serine 14 (S14) and Serine 17 (S17) are known regulators of Cdc37 activity.
  • The comprehensive impact of phosphorylation across the entire Cdc37 protein remains largely unexplored.

Purpose of the Study:

  • To systematically investigate the functional consequences of phosphorylation at all potential sites across the Cdc37 protein.
  • To identify novel phosphorylation sites regulating Cdc37 function under various cellular conditions.
  • To establish a resource for understanding the role of Cdc37 post-translational modifications in cellular proteostasis and disease.

Main Methods:

  • Creation of a comprehensive "Cdc37 code collection" comprising 46 yeast strains, each expressing a single phospho-site mutant of Cdc37.
  • Extensive phenotypic profiling of these mutant strains across a broad spectrum of environmental and chemical stressors.
  • Comparative analysis of stress response phenotypes to identify unique and overlapping regulatory roles of different phosphorylation sites.

Main Results:

  • Canonical phosphorylation sites (S14, S17) are confirmed as essential for stress tolerance.
  • 34 novel phospho-mutants exhibited distinct and stress-specific phenotypes, indicating diverse regulatory roles.
  • Minimal overlap in stress responses among the novel mutants suggests modular and context-dependent regulation of Cdc37 function.
  • Site-specific phosphorylation intricately modulates Cdc37's capacity to maintain proteostasis under diverse cellular challenges.

Conclusions:

  • Cdc37 function is extensively modulated by site-specific phosphorylation, impacting its role in maintaining proteostasis.
  • The study identifies numerous novel regulatory phosphorylation sites on Cdc37, expanding our understanding of its post-translational regulation.
  • These findings provide a valuable resource for future research into the chaperone-kinase network and its dysregulation in disease states.