Evidence map›Paper›PMID 28827405›Full record

ArticleJournal of cell science2017

Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex formation for ER-associated degradation (ERAD).

Jasmin Schulz, Dönem Avci, Markus A Queisser, Aljona Gutschmidt, Lena-Sophie Dreher, Emma J Fenech, Norbert Volkmar, Yuki Hayashi, Thorsten Hoppe, John C Christianson

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 10% 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

53 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.

  1. Pooled it
  2. Article
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  5. Review
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  10. Vitamin BResearch square · 2025
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  13. Article
  14. Review
  15. Review
  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

10 authors at 3 institutions in 3 countries.

Jasmin SchulzLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7DQ, UK.
Dönem AvciLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7DQ, UK.ORCID http://orcid.org/0000-0003-2506-1670
Markus A QueisserLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7DQ, UK.ORCID http://orcid.org/0000-0002-3368-3827
Aljona GutschmidtInstitute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne 50931, Germany.ORCID http://orcid.org/0000-0002-2165-2126
Lena-Sophie DreherInstitute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne 50931, Germany.
Emma J FenechLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7DQ, UK.
Norbert VolkmarLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7DQ, UK.
Yuki HayashiDepartment of Pharmaceutical Sciences, University of Tokyo, Tokyo 113-0033, Japan.
Thorsten HoppeInstitute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne 50931, Germany.ORCID http://orcid.org/0000-0002-4734-9352
John C ChristiansonLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7DQ, UK john.christianson@ludwig.ox.ac.uk.ORCID http://orcid.org/0000-0002-0474-1207
University of Oxford · GBUniversity of Cologne · DEThe University of Tokyo · JP

Funding

European Research Council 616499Medical Research Council MR/L001209/1
6 · The paper itself

Abstract

The mammalian ubiquitin ligase Hrd1 is the central component of a complex facilitating degradation of misfolded proteins during the ubiquitin-proteasome-dependent process of ER-associated degradation (ERAD). Hrd1 associates with cofactors to execute ERAD, but their roles and how they assemble with Hrd1 are not well understood. Here, we identify crucial cofactor interaction domains within Hrd1 and report a previously unrecognised evolutionarily conserved segment within the intrinsically disordered cytoplasmic domain of Hrd1 (termed the HAF-H domain), which engages complementary segments in the cofactors FAM8A1 and Herp (also known as HERPUD1). This domain is required by Hrd1 to interact with both FAM8A1 and Herp, as well as to assemble higher-order Hrd1 complexes. FAM8A1 enhances binding of Herp to Hrd1, an interaction that is required for ERAD. Our findings support a model of Hrd1 complex formation, where the Hrd1 cytoplasmic domain and FAM8A1 have a central role in the assembly and activity of this ERAD machinery.

Indexed as

Models, BiologicalEndoplasmic Reticulum-Associated DegradationHEK293 CellsHumansMembrane ProteinsUbiquitin-Protein LigasesFAM8A1 protein, humanHERPUD1 protein, humanMembrane ProteinsSYVN1 protein, humanUbiquitin-Protein LigasesE3 ubiquitin ligaseEndoplasmic reticulum (ER)ER-associated degradationER quality controlFAM8A1HerpOligomerisationProtein complex

Identifiers

PMID28827405
PMCPMC5665440
OpenAlexW2749644250

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.