Evidence map›Paper›PMID 29109265›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

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

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

Abstract read
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In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.3field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 15 citations in OpenAlex.

  1. Glycoproteome remodeling and organelle-specificProceedings of the National Academy of Sciences of the United States of America · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Kofi L P StevensSchool of Biomedical Sciences, Faculty of Health Sciences, Curtin University, Bentley, WA 6102, Australia.
Amy L BlackSchool of Biomedical Sciences, Faculty of Health Sciences, Curtin University, Bentley, WA 6102, Australia.
Kelsi M WellsSchool of Biomedical Sciences, Faculty of Health Sciences, Curtin University, Bentley, WA 6102, Australia.
K Y Benjamin YeoSchool of Chemistry and Molecular Biosciences, Faculty of Science, University of Queensland, Brisbane St Lucia, QLD 4072, Australia.
Robert F L SteuartCurtin Health Innovation Research Institute and Faculty of Health Sciences, Curtin University, Bentley, WA 6102, Australia.
Colin J StirlingFaculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.
Benjamin L SchulzSchool of Chemistry and Molecular Biosciences, Faculty of Science, University of Queensland, Brisbane St Lucia, QLD 4072, Australia.
Carl J MousleySchool of Biomedical Sciences, Faculty of Health Sciences, Curtin University, Bentley, WA 6102, Australia; carl.mousley@curtin.edu.au.
Curtin University · AUUniversity of Queensland · AUUniversity of Manchester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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 Lhs1, is diminished upon reductive stress. N-glycosylation of Sil1 is predominantly Ost3-dependent and requires a functional Ost3 CxxC thioredoxin motif. N-glycosylation of Lhs1 is largely Ost3-independent and independent of the CxxC motif. Unglycosylated Sil1 is not only functional but is more effective at rescuing loss of Lhs1 activity than N-glycosylated Sil1. Furthermore, substitution of the redox active cysteine pair C52 and C57 in the N terminus of Sil1 results in the Doa10-dependent ERAD of this mutant protein. We propose that reductive stress in the ER inhibits the Ost3-dependent N-glycosylation of Sil1, which regulates specific BiP functions appropriate to the needs of the ER under reductive stress.

Indexed as

Gene Expression Regulation, FungalProtein Processing, Post-TranslationalAmino Acid MotifsAmino Acid SubstitutionEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationEndoplasmic Reticulum StressFungal ProteinsGlycosylationHexosyltransferasesHSP70 Heat-Shock ProteinsHydrogen PeroxideMembrane ProteinsMembrane Transport ProteinsMutationOxidation-Reductiondolichyl-diphosphooligosaccharide - protein glycotransferaseFungal ProteinsHexosyltransferasesHSP70 Heat-Shock ProteinsHydrogen PeroxideKAR2 protein, yeastLHS1 protein, S cerevisiaeMembrane ProteinsMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsSIL1 protein, S cerevisiaeSSM4 protein, S cerevisiaeThioredoxinsUbiquitin-Protein LigasesERADN-glycosylationOst3redoxSil1

Identifiers

PMID29109265
PMCPMC5703277
OpenAlexW2767914285

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.