Evidence map›Paper›PMID 27321670›Full record

ArticleCell2016

Autoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD.

Ryan D Baldridge, Tom A Rapoport

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
16.3field-weighted citation impact, top 1% 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

128 citing papers in PubMed, 202 citations in OpenAlex.

  1. Article
  2. Review
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  5. Review
  6. Competition between Der1 and ERAD-M substrates controls Hrd1 complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Article
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  12. SEL1L-HRD1-mediated ERAD in mammals.Nature cell biology · 2025
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. ER-associated degradation ligase HRD1 links ER stress to DNA damage repair by modulating the activity of DNA-PKcs.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

68 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Ryan D BaldridgeHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. Electronic address: ryan_baldridge@hms.harvard.edu.
Tom A RapoportHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. Electronic address: tom_rapoport@hms.harvard.edu.
Harvard University · USHoward Hughes Medical Institute · US

Funding

PROTEIN TRANSPORT INTO MAMMALIAN ENDOPLASMIC RETICULUMR01GM052586 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Tom A Rapoport · 1995 to 2026
$11.9M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM052586
6 · The paper itself

Abstract

Misfolded proteins of the ER are retrotranslocated to the cytosol, where they are polyubiquitinated, extracted from the membrane, and degraded by the proteasome. To investigate how the ER-associated Degradation (ERAD) machinery can accomplish retrotranslocation of a misfolded luminal protein domain across a lipid bilayer, we have reconstituted retrotranslocation with purified S. cerevisiae proteins, using proteoliposomes containing the multi-spanning ubiquitin ligase Hrd1. Retrotranslocation of the luminal domain of a membrane-spanning substrate is triggered by autoubiquitination of Hrd1. Substrate ubiquitination is a subsequent event, and the Cdc48 ATPase that completes substrate extraction from the membrane is not required for retrotranslocation. Ubiquitination of lysines in Hrd1's RING-finger domain is required for substrate retrotranslocation in vitro and for ERAD in vivo. Our results suggest that Hrd1 forms a ubiquitin-gated protein-conducting channel.

Indexed as

Endoplasmic Reticulum-Associated DegradationProtein FoldingAdenosine TriphosphatasesCell Cycle ProteinsEndoplasmic ReticulumProteolipidsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationUbiquitin-Protein LigasesValosin Containing ProteinAdenosine TriphosphatasesCDC48 protein, S cerevisiaeCell Cycle ProteinsHRD1 protein, S cerevisiaeProteolipidsproteoliposomesSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesValosin Containing Protein

Identifiers

PMID27321670
PMCPMC4946995
OpenAlexW2442194410

What OpenQuestion holds

Textmetadata
LicenceTDM
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.