Evidence map›Paper›PMID 27570074›Full record

ArticleMolecular cell2016

Posttranscriptional Regulation of Glycoprotein Quality Control in the Endoplasmic Reticulum Is Controlled by the E2 Ub-Conjugating Enzyme UBC6e.

Masatoshi Hagiwara, Jingjing Ling, Paul-Albert Koenig, Hidde L Ploegh

Open access · greenAbstract read
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Turnover of EDEM1, an ERAD-enhancing factor, is mediated by multiple degradation routes.Genes to cells : devoted to molecular & cellular mechanisms · 2024
    Article
  4. Review
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  6. Article
  7. Review
  8. Article
  9. Article
  10. Endoplasmic Reticulum Protein Quality Control in β Cells.Seminars in cell & developmental biology · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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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

4 authors at 1 institution in 1 country.

Masatoshi HagiwaraWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
Jingjing LingWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
Paul-Albert KoenigWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
Hidde L PloeghWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA. Electronic address: ploegh@wi.mit.edu.
Whitehead Institute for Biomedical Research · US

Funding

A new strategy to disrupt protein-protein interactions in eukaryotic cells.DP1GM106409 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PLOEGH, HIDDE L. · 2012 to 2016
$4.8M
Sortase-mediated protein engineering for the study of host-pathogen interactionsR01AI087879 · NIAID · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PLOEGH, HIDDE L. · 2010 to 2019
$4.5M
NIAID NIH HHS R01 AI087879NIGMS NIH HHS DP1 GM106409
6 · The paper itself

Abstract

ER-associated degradation (ERAD) is essential for protein quality control in the ER, not only when the ER is stressed, but also at steady state. We report a new layer of homeostatic control, in which ERAD activity itself is regulated posttranscriptionally and independently of the unfolded protein response by adjusting the endogenous levels of EDEM1, OS-9, and SEL1L (ERAD enhancers). Functional UBC6e requires its precise location in the ER to form a supramolecular complex with Derlin2. This complex targets ERAD enhancers for degradation, a function that depends on UBC6e's enzymatic activity. Ablation of UBC6e causes upregulation of active ERAD enhancers and so increases clearance not only of terminally misfolded substrates, but also of wild-type glycoproteins that fold comparatively slowly in vitro and in vivo. The levels of proteins that comprise the ERAD machinery are thus carefully tuned and adjusted to prevailing needs.

Indexed as

Protein Processing, Post-TranslationalAnimalsEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationFibroblastsGenetic VectorsGlycosylationHEK293 CellsHumansLectinsLentivirusMembrane ProteinsMiceNeoplasm ProteinsProteinsProteolysisDERL2 protein, humanEDEM1 protein, humanLectinsMembrane ProteinsNeoplasm ProteinsOS9 protein, humanProteinsSEL1L protein, humanUBE2J1 protein, humanUbiquitin-Conjugating Enzymes

Identifiers

PMID27570074
PMCPMC5010495
OpenAlexW2513769973

What OpenQuestion holds

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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.