Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

With or Without You: Co-chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage

Version 1 : Received: 9 October 2021 / Approved: 11 October 2021 / Online: 11 October 2021 (14:38:49 CEST)

A peer-reviewed article of this Preprint also exists.

Altinok, S.; Sanchez-Hodge, R.; Stewart, M.; Smith, K.; Schisler, J.C. With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage. Cells 2021, 10, 3121. Altinok, S.; Sanchez-Hodge, R.; Stewart, M.; Smith, K.; Schisler, J.C. With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage. Cells 2021, 10, 3121.

Journal reference: Cells 2021, 10, 3121
DOI: 10.3390/cells10113121

Abstract

Heat shock proteins (HSPs) are a family of molecular chaperones that regulate essential protein refolding and triage decisions to maintaining protein homeostasis. Numerous co-chaperone proteins directly interact and modify the function of HSPs, and these interactions impact the outcome of protein triage, impacting everything from structural proteins to cell signaling mediators. The chaperone/co-chaperone machinery protects against various stressors to ensuring cellular function in the face of stress. However, coding mutations, expression changes, and post-translational modifications of the chaperone/co-chaperone machinery can alter the cellular stress response. Importantly, these dysfunctions appear to contribute to numerous human diseases. Therapeutic targeting of chaperones is an attractive but challenging approach due to the vast functions of HSPs, likely contributing to the off-target effects of these therapies. Current efforts focus on targeting co-chaperones to develop precise treatments for numerous diseases caused by defects in protein quality control. This review focuses on the recent developments regarding selected HSP70/HSP90 co-chaperones, focusing on cardioprotection, neuroprotection, and cancer. We also discuss therapeutic approaches that highlight both the utility and challenges of targeting co-chaperones.

Keywords

heat shock proteins; co-chaperones; protein quality control; protein folding; protein degradation; cardioprotection; neuroprotection; cancer

Subject

LIFE SCIENCES, Cell & Developmental Biology

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