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Chaperome heterogeneity and its implications for cancer study and treatment

Content Provider	Scilit
Author	Wang, Tai Rodina, Anna Dunphy, Mark P. Corben, Adriana Modi, Shanu Guzman, Monica L. Gewirth, Daniel T. Chiosis, Gabriela
Copyright Year	2019
Description	Journal: Journal of Biological Chemistry The chaperome is the collection of proteins in the cell that carry out molecular chaperoning functions. Changes in the interaction strength between chaperome proteins lead to an assembly that is functionally and structurally distinct from each constituent member. In this review, we discuss the epichaperome, the cellular network that forms when the chaperome components of distinct chaperome machineries come together as stable, functionally integrated, multimeric complexes. In tumors, maintenance of the epichaperome network is vital for tumor survival, rendering them vulnerable to therapeutic interventions that target critical epichaperome network components. We discuss how the epichaperome empowers an approach for precision medicine cancer trials where a new target, biomarker, and relevant drug candidates can be correlated and integrated. We introduce chemical biology methods to investigate the heterogeneity of the chaperome in a given cellular context. Lastly, we discuss how ligand–protein binding kinetics are more appropriate than equilibrium binding parameters to characterize and unravel chaperome targeting in cancer and to gauge the selectivity of ligands for specific tumor-associated chaperome pools.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6369301/pdf http://www.jbc.org/content/294/6/2162.full.pdf
Ending Page	2179
Page Count	18
Starting Page	2162
ISSN	00219258
e-ISSN	1083351X
DOI	10.1074/jbc.rev118.002811
Journal	Journal of Biological Chemistry
Issue Number	6
Volume Number	294
Language	English
Publisher	Elsevier BV
Publisher Date	2019-02-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Chemistry Medicinal Chemistry 70 Kilodalton Heat Shock Protein (hsp70) Heat Shock Protein 90 (hsp90)
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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