biostudies-literatureRodina ANCATS NIH HHSNIA NIH HHSNCRR NIH HHSNIAID NIH HHSNIMH NIH HHSNCI NIH HHSNINDS NIH HHSNIH HHS397-401https://www.ebi.ac.uk/biostudies/studies/S-EPMC5283383biostudies-literatureUnknown538(7625)Transient, multi-protein complexes are important facilitators of cellular functions. This includes the chaperome, an abundant protein family comprising chaperones, co-chaperones, adaptors, and folding enzymes-dynamic complexes of which regulate cellular homeostasis together with the protein degradation machinery. Numerous studies have addressed the role of chaperome members in isolation, yet little is known about their relationships regarding how they interact and function together in malignancy. As function is probably highly dependent on endogenous conditions found in native tumours, chaperomes have resisted investigation, mainly due to the limitations of methods needed to disrupt or engineer the cellular environment to facilitate analysis. Such limitations have led to a bottleneck in ouNatureThe epichaperome is an integrated chaperome network that facilitates tumour survival.PMC5283383F32 CA192786R03 NS050838R21 AI090501UL1 TR002384P30 CA008748P01 CA186866UL1 TR000457R21 CA158609R01 CA103646P50 CA192937R21 AG028811R01 CA119001R01 CA172546U01 AG032969DP2 OD007399UL1 RR024996P50 CA086438R03 MH076499R01 CA155226Lin OMelnick APeter RIPressl CPanchal PStuder LGomes EDAlpaugh MShimizu FModi SCesarman ELarson SMPillarsetty NKoren JRiolo MZong HPatil SKishinevsky SWang TChu FCorben AErdjument-Bromage HGerecitano JFBeattie BZanzonico PRodina AYan PCaldas-Lopes ETrondl RXu CDunphy MPYang CTaldone TRoboz GJLevine RPatel HJFarooq MFGuzman MLChiosis GLewis JSCerchietti LBolaender AHudis CfalseThe epichaperome is an integrated chaperome network that facilitates tumour survival.Transient, multi-protein complexes are important facilitators of cellular functions. This includes the chaperome, an abundant protein family comprising chaperones, co-chaperones, adaptors, and folding enzymes-dynamic complexes of which regulate cellular homeostasis together with the protein degradation machinery. Numerous studies have addressed the role of chaperome members in isolation, yet little is known about their relationships regarding how they interact and function together in malignancy. As function is probably highly dependent on endogenous conditions found in native tumours, chaperomes have resisted investigation, mainly due to the limitations of methods needed to disrupt or engineer the cellular environment to facilitate analysis. Such limitations have led to a bottleneck in ou2016-01-01T00:00:00Z2016 Oct2025-04-18T17:46:05.872Z2019-03-27T02:35:20ZS-EPMC52833832770613510.1038/nature19807