Evidence map›Paper›PMID 24478453›Full record

ArticleMolecular biology of the cell2014

Herp coordinates compartmentalization and recruitment of HRD1 and misfolded proteins for ERAD.

Julia Leitman, Marina Shenkman, Yana Gofman, Navit Ogen Shtern, Nir Ben-Tal, Linda M Hendershot, Gerardo Z Lederkremer

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

47 citing papers in PubMed, 85 citations in OpenAlex.

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  17. Thapsigargin: key to new host-directed coronavirus antivirals?Trends in pharmacological sciences · 2022
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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

7 authors at 2 institutions in 2 countries.

Julia LeitmanDepartment of Cell Research and Immunology, George Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel Department of Biochemistry and Molecular Biology, George Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, TN 38105.
Marina Shenkman
Yana Gofman
Navit Ogen Shtern
Nir Ben-Tal
Linda M Hendershot
Gerardo Z Lederkremer
Tel Aviv University · ILSt. Jude Children's Research Hospital · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A functional unfolded protein response (UPR) is essential for endoplasmic reticulum (ER)-associated degradation (ERAD) of misfolded secretory proteins, reflecting the fact that some level of UPR activation must exist under normal physiological conditions. A coordinator of the UPR and ERAD processes has long been sought. We previously showed that the PKR-like, ER-localized eukaryotic translation initiation factor 2α kinase branch of the UPR is required for the recruitment of misfolded proteins and the ubiquitin ligase HRD1 to the ER-derived quality control compartment (ERQC), a staging ground for ERAD. Here we show that homocysteine-induced ER protein (Herp), a protein highly upregulated by this UPR branch, is responsible for this compartmentalization. Herp localizes to the ERQC, and our results suggest that it recruits HRD1, which targets to ERAD the substrate presented by the OS-9 lectin at the ERQC. Predicted overall structural similarity of Herp to the ubiquitin-proteasome shuttle hHR23, but including a transmembrane hairpin, suggests that Herp may function as a hub for membrane association of ERAD machinery components, a key organizer of the ERAD complex.

Indexed as

Cell CompartmentationEndoplasmic Reticulum-Associated DegradationProtein FoldingAnimalsCell LineCell MembraneDNA-Binding ProteinsDNA Repair EnzymesEndoplasmic ReticulumEukaryotic Initiation Factor-2Gene Knockdown TechniquesGlycosylationHumansLectinsMembrane ProteinsMiceDNA-Binding ProteinsDNA Repair EnzymesEukaryotic Initiation Factor-2Herpud1 protein, mouseLectinsMembrane ProteinsMutant ProteinsRAD23A protein, humanSYVN1 protein, humanTranscription Factor CHOPUbiquitin-Protein Ligases

Identifiers

PMID24478453
PMCPMC3967970
OpenAlexW2144104591

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.