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.
[doi:10.25345/C5N99X]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: GRP94, N-Glycosylation, protein-protein interactions
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Thomas A. Neubert, New York Unversity School of Medicine, USA |
Submitting User: | gc_lab_2016 |
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