A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.

ABSTRACT: Chaperones are abundant cellular proteins that promote the folding and function of their substrate proteins (clients). In vivo, chaperones also associate with a large and diverse set of cofactors (cochaperones) that regulate their specificity and function. However, how these cochaperones regulate protein folding and whether they have chaperone-independent biological functions is largely unknown. We combined mass spectrometry and quantitative high-throughput LUMIER assays to systematically characterize the chaperone-cochaperone-client interaction network in human cells. We uncover hundreds of chaperone clients, delineate their participation in specific cochaperone complexes, and establish a surprisingly distinct network of protein-protein interactions for cochaperones. As a salient example

SUBMITTER: Taipale M 

PROVIDER: S-EPMC4104544 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature