Evidence map›Paper›PMID 27325793›Full record

ArticleThe Journal of cell biology2016

Limited ER quality control for GPI-anchored proteins.

Natalia Sikorska, Leticia Lemus, Auxiliadora Aguilera-Romero, Javier Manzano-Lopez, Howard Riezman, Manuel Muñiz, Veit Goder

Abstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

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  12. New frontiers in quality control: the case of GPI-anchored proteins.Nature reviews. Molecular cell biology · 2023
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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.

Natalia SikorskaDepartment of Genetics, University of Seville, 41012 Seville, Spain.ORCID 0000-0003-3333-697X
Leticia LemusDepartment of Genetics, University of Seville, 41012 Seville, Spain.
Auxiliadora Aguilera-RomeroNational Centre of Competence in Research, Chemical Biology, Sciences II, University of Geneva, 1211 Geneva 4, Switzerland Department of Biochemistry, Sciences II, University of Geneva, 1211 Geneva 4, Switzerland.
Javier Manzano-LopezDepartment of Cell Biology, University of Seville, 41012 Seville, Spain Instituto de Biomedicina de Sevilla, Hospital Universitario Virgen del Rocío, Consejo Superior de Investigaciones Científicas, University of Seville, 41013 Seville, Spain.ORCID 0000-0002-7149-1690
Howard RiezmanNational Centre of Competence in Research, Chemical Biology, Sciences II, University of Geneva, 1211 Geneva 4, Switzerland Department of Biochemistry, Sciences II, University of Geneva, 1211 Geneva 4, Switzerland.ORCID 0000-0003-4680-9422
Manuel MuñizDepartment of Cell Biology, University of Seville, 41012 Seville, Spain Instituto de Biomedicina de Sevilla, Hospital Universitario Virgen del Rocío, Consejo Superior de Investigaciones Científicas, University of Seville, 41013 Seville, Spain.ORCID 0000-0001-8011-6991
Veit GoderDepartment of Genetics, University of Seville, 41012 Seville, Spain vgoder@us.es.ORCID 0000-0003-0854-4873

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endoplasmic reticulum (ER) quality control mechanisms target terminally misfolded proteins for ER-associated degradation (ERAD). Misfolded glycophosphatidylinositol-anchored proteins (GPI-APs) are, however, generally poor ERAD substrates and are targeted mainly to the vacuole/lysosome for degradation, leading to predictions that a GPI anchor sterically obstructs ERAD. Here we analyzed the degradation of the misfolded GPI-AP Gas1* in yeast. We could efficiently route Gas1* to Hrd1-dependent ERAD and provide evidence that it contains a GPI anchor, ruling out that a GPI anchor obstructs ERAD. Instead, we show that the normally decreased susceptibility of Gas1* to ERAD is caused by canonical remodeling of its GPI anchor, which occurs in all GPI-APs and provides a protein-independent ER export signal. Thus, GPI anchor remodeling is independent of protein folding and leads to efficient ER export of even misfolded species. Our data imply that ER quality control is limited for the entire class of GPI-APs, many of them being clinically relevant.

Indexed as

Endoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationFungal ProteinsGlycosylphosphatidylinositolsProtein BindingProtein FoldingYeastsFungal ProteinsGlycosylphosphatidylinositolsplasmanylinositol glycan

Identifiers

PMID27325793
PMCPMC4915193

What OpenQuestion holds

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Registered trials

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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.