Molecular Chaperones: Guardians of Tumor Suppressor Stability

“Focusing on the holistic lifecycle of these proteins reveals commonalities between the widely diverse group of tumor suppressors, which is invaluable to inform therapy development for multiple cancers.”

BUFFALO, NY- October 16, 2024 – A new review was published in Oncotarget's Volume 15 on October 1, 2024, entitled, “Molecular chaperones: Guardians of tumor suppressor stability and function.”

As highlighted in the abstract of this paper, "tumor suppressor" describes a diverse set of genes typically involved in suppressing metastasis, but which can lead to tumorigenesis when loss-of-function mutations occur. Despite the varied structures and functions of tumor suppressor proteins, many share a common regulatory mechanism—they are "clients" of molecular chaperones, and they rely on an intracellular network of chaperones and co-chaperones to maintain their stability. Mutations in tumor suppressors that disrupt proper chaperoning prevent cells from maintaining sufficient protein levels for normal physiological function.

In their review, researchers Jennifer A. Heritz, Sarah J. Backe, and Mehdi Mollapour from SUNY Upstate Medical University and New York VA Health Care in Syracuse, New York, discuss the role of molecular chaperones Hsp70 and Hsp90 in maintaining the stability and functional integrity of tumor suppressors. They also detail the contributions of co-chaperones prefoldin, HOP, Aha1, p23, FNIP1/2, and Tsc1, as well as the chaperonin TRiC, to tumor suppressor stability.

“Overall, it is clear that oncogenesis can result from the dysregulation of tumor suppressor stabilization by chaperones.”

Continue reading: DOI: https://doi.org/10.18632/oncotarget.28653

Correspondence to: Mehdi Mollapour - mollapom@upstate.edu

Keywords: cancer, molecular chaperone, tumor suppressor, renal cell carcinoma, Birt-Hogg-Dubé (BHD) syndrome, TSC syndrome

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