Evidence map›Paper›PMID 25583996›Full record

ArticleThe Journal of cell biology2015

The Erv41-Erv46 complex serves as a retrograde receptor to retrieve escaped ER proteins.

Aya Shibuya, Neil Margulis, Romain Christiano, Tobias C Walther, Charles Barlowe

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  8. Conventional and Unconventional Protein Secretion in Yeast and Animal Cells.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  9. The Endoplasmic Reticulum and the Fidelity of Nascent Protein Localization.Cold Spring Harbor perspectives in biology · 2023
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Aya ShibuyaDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755.
Neil MargulisDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755.
Romain ChristianoDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520.
Tobias C WaltherDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520.
Charles BarloweDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755 barlowe@dartmouth.edu.
Dartmouth College · USYale University · US

Funding

Mechanisms of COPII-dependent TransportR01GM052549 · NIGMS · DARTMOUTH COLLEGE · PI BARLOWE, CHARLES K · 1995 to 2024
$7.2M
Mechanisms of COPII-Dependent TransportR37GM052549 · NIGMS · DARTMOUTH COLLEGE · PI BARLOWE, CHARLES K · 2007 to 2016
$5.3M
Mechanisms of Lipid Droplet Protein TargetingR01GM097194 · NIGMS · YALE UNIVERSITY · PI WALTHER, TOBIAS C · 2011 to 2024
$4.9M
Cellular Functions of Plasma Membrane Organization by EisosomesR01GM095982 · NIGMS · YALE UNIVERSITY · PI WALTHER, TOBIAS C · 2012 to 2015
$1.2M
NIGMS NIH HHS GM052549NIGMS NIH HHS GM095982NIGMS NIH HHS GM097194NIGMS NIH HHS R01 GM052549NIGMS NIH HHS R01 GM095982NIGMS NIH HHS R01 GM097194NIGMS NIH HHS R37 GM052549
6 · The paper itself

Abstract

Signal-dependent sorting of proteins in the early secretory pathway is required for dynamic retention of endoplasmic reticulum (ER) and Golgi components. In this study, we identify the Erv41-Erv46 complex as a new retrograde receptor for retrieval of non-HDEL-bearing ER resident proteins. In cells lacking Erv41-Erv46 function, the ER enzyme glucosidase I (Gls1) was mislocalized and degraded in the vacuole. Biochemical experiments demonstrated that the luminal domain of Gls1 bound to the Erv41-Erv46 complex in a pH-dependent manner. Moreover, in vivo disturbance of the pH gradient across membranes by bafilomycin A1 treatment caused Gls1 mislocalization. Whole cell proteomic analyses of deletion strains using stable isotope labeling by amino acids in culture identified other ER resident proteins that depended on the Erv41-Erv46 complex for efficient localization. Our results support a model in which pH-dependent receptor binding of specific cargo by the Erv41-Erv46 complex in Golgi compartments identifies escaped ER resident proteins for retrieval to the ER in coat protein complex I-formed transport carriers.

Indexed as

alpha-GlucosidasesEndoplasmic ReticulumHydrogen-Ion ConcentrationMembrane ProteinsProtein BindingProtein Interaction MappingProtein TransportProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesalpha-GlucosidasesErv41 protein, S cerevisiaeErv46 protein, S cerevisiaeglucosidase IMembrane ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID25583996
PMCPMC4298680
OpenAlexW2121848043

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.