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Changes in the strength of protein-protein interactions portend oncogenic activity and generate actionable targets for cancer

ABSTRACT: Stresses associated with disease may pathologically remodel the cellular proteins by increasing the interaction strength between chaperome members, and between the chaperome and the proteins it regulates. How these changes in protein-protein interaction strength are executed remains unknown. Our study shows that the ER chaperone GRP94 employs a specific glycosylation pattern to alter its conformational fitness and to stabilize a state most permissive for stable interactions with proteins at the plasma membrane.

INSTRUMENT(S): Q Exactive (Thermo Scientific instrument model HF)

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Thomas A. Neubert

PROVIDER: MSV000085459 | MassIVE | Fri May 22 13:30:00 BST 2020

REPOSITORIES: MassIVE

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