Drs. Mehdi Mollapour, Jennifer Heritz, and Sarah Backe from SUNY Upstate Medical University (Syracuse, NY) discuss a review they co-authored that was published by Oncotarget in Volume 15, entitled, “Molecular chaperones: Guardians of tumor suppressor stability and function.”
DOI - https://doi.org/10.18632/oncotarget.28653
Correspondence to - Mehdi Mollapour - mollapom@upstate.edu
Video interview - https://www.youtube.com/watch?v=vEHmyemWgNo
Video transcript - https://www.oncotarget.net/2024/10/24/behind-the-study-molecular-chaperones-tumor-suppressor-stability/
Abstract
The term ‘tumor suppressor’ describes a widely diverse set of genes that are generally involved in the suppression of metastasis, but lead to tumorigenesis upon loss-of-function mutations. Despite the protein products of tumor suppressors exhibiting drastically different structures and functions, many share a common regulatory mechanism—they are molecular chaperone ‘clients’. Clients of molecular chaperones depend on an intracellular network of chaperones and co-chaperones to maintain stability. Mutations of tumor suppressors that disrupt proper chaperoning prevent the cell from maintaining sufficient protein levels for physiological function. This review discusses the role of the molecular chaperones Hsp70 and Hsp90 in maintaining the stability and functional integrity of tumor suppressors. The contribution of cochaperones prefoldin, HOP, Aha1, p23, FNIP1/2 and Tsc1 as well as the chaperonin TRiC to tumor suppressor stability is also discussed. Genes implicated in renal cell carcinoma development—VHL, TSC1/2, and FLCN—will be used as examples to explore this concept, as well as how pathogenic mutations of tumor suppressors cause disease by disrupting protein chaperoning, maturation, and function.
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Keywords - cancer, molecular chaperone, tumor suppressor, renal cell carcinoma, Birt-Hogg-Dubé (BHD) syndrome, TSC syndrome
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