Fig. 1: Epichaperomics identifies epichaperomes involved in the fitness of mitotic protein pathways in cancer.
From: Epichaperomics reveals dysfunctional chaperone protein networks
Schematic representation of applying epichaperomics to identify protein–protein interaction complexes, also known as epichaperomes, in cancer. epiHsp70s and epiHsp90s consist of heterooligomers that can be detected, isolated, and quantified by several chemical probes. epiHsp70s and epiHsp90s are context-dependent regulators of mitotic cell cycle checkpoints in cancer. An array of post-translational modifications of epiHsp70s and epiHsp90s, also known as the chaperone code, may play a role in the formation of epichaperomes in cancer. Molecular chaperones include Hsp70, Hsc70, Hsp90α, Hsp90β, Hsp40, and Hsp110. Co-chaperones include Hop, Aha1, and Cdc37.
