Dr. Samuel Silva from the Department of Pathology at Federal University of Ceará in Fortaleza, Brazil

Samuel Silva from the Department of Pathology at Federal University of Ceará in Fortaleza, Brazil, discusses a research paper he co-authored that was published in Oncotarget Volume 15, titled, “Relationship between the expressions of DLL3, ASC1, TTF-1 and Ki-67: First steps of precision medicine at SCLC.”

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.

DOI - https://doi.org/10.18632/oncotarget.28660

Full text - https://www.oncotarget.com/article/28660/text/

Correspondence to - Fabio Tavora - [email protected]

Keywords - cancer, DLL3, pathology, biomarkers, qupath, small cell carcinoma