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Article

Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.

Proceedings of the National Academy of Sciences of the United States of America - 21 Nov 2017

Stevens Kofi L P, Black Amy L, Wells Kelsi M, Yeo K Y Benjamin, Steuart Robert F L, Stirling Colin J, Schulz Benjamin L, Mousley Carl J

Abstract excerpt

BiP (Kar2 in yeast) is an essential Hsp70 chaperone and master regulator of endoplasmic reticulum (ER) function. BiP's activity is regulated by its intrinsic ATPase activity that can be stimulated by two different nucleotide exchange factors, Sil1 and Lhs1. Both Sil1 and Lhs1 are glycoproteins, but how N-glycosylation regulates their function is not known. Here, we show that N-glycosylation of Sil1, but not of...

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Identifiers

PMID: 29109265
DOI: 10.1073/pnas.1705641114
PMCID: PMC5703277

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.PMID 29109265Read ↗

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