The HSP90 chaperone code regulates the crosstalk between proteostasis and autophagy

ABSTRACT

Proteostasis, the maintenance of proper protein folding, stability, and degradation within cells, is fundamental for cellular function. Two key players in this intricate cellular process are macroautophagy/autophagy and chaperoning of nascent proteins. Here, we explore the crosstalk between autophagy and the HSP90 chaperone in maintaining proteostasis, highlighting their interplay and significance in cellular homeostasis.

Abbreviation: HSP90: heat shock protein 90; PTMs: post-translational modifications

KEYWORDS:

• Atg1
• chaperone
• chaperone code
• co-chaperone
• phosphorylation
• ULK1

Acknowledgements

The content is solely the responsibility of the authors and does not necessarily represent the official views of the NIH. This work was also supported with funds from the SUNY Upstate Medical University, Upstate Foundation. Schematics in Figure 1 was created with BioRender.com.

Disclosure statement

No potential conflict of interest was reported by the author(s).

Additional information

Funding

This work was supported by the National Institute of General MedicalSciences of the National Institutes of Health (NIH) under [Award Number R35GM139584] (M.M.).