XBP1s Links the Unfolded Protein Response to the Molecular Architecture of Mature N-Glycans.

ABSTRACT: The molecular architecture of the mature N-glycome is dynamic, with consequences for both normal and pathologic processes. Elucidating cellular mechanisms that modulate the N-linked glycome is, therefore, crucial. The unfolded protein response (UPR) is classically responsible for maintaining proteostasis in the secretory pathway by defining levels of chaperones and quality control proteins. Here, we employ chemical biology methods for UPR regulation to show that stress-independent activation of the UPR's XBP1s transcription factor also induces a panel of N-glycan maturation-related enzymes. The downstream consequence is a distinctive shift toward specific hybrid and complex N-glycans on N-glycoproteins produced from XBP1s-activated cells, which we characterize by mass spectrometry. Pulse-c

SUBMITTER: Dewal MB 

PROVIDER: S-EPMC4621487 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature