Evidence map›Paper›PMID 29809151›Full record

ArticleeLife2018

The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins.

Matthew J Shurtleff, Daniel N Itzhak, Jeffrey A Hussmann, Nicole T Schirle Oakdale, Elizabeth A Costa, Martin Jonikas, Jimena Weibezahn, Katerina D Popova, Calvin H Jan, Pavel Sinitcyn and 8 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed
11.9field-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

142 citing papers in PubMed, 241 citations in OpenAlex.

  1. Article
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  4. Role of Pbr1, a putative oxidoreductase, in the ER quality control and folding of yeast Fks1 glucan synthase.Proceedings of the National Academy of Sciences of the United States of America · 2026
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82 more citing papers are in PubMed but not listed here.

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

18 authors at 4 institutions in 2 countries.

Matthew J Shurtleff *Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States.ORCID http://orcid.org/0000-0001-9846-3051
Daniel N Itzhak *Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Jeffrey A HussmannDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States.
Nicole T Schirle OakdaleDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States.
Elizabeth A CostaDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States.ORCID http://orcid.org/0000-0001-8365-0436
Martin JonikasDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States.
Jimena WeibezahnDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States.
Katerina D PopovaDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States.
Calvin H JanDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States.
Pavel SinitcynDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID https://orcid.org/0000-0002-2653-1702
Shruthi S VembarDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, United States.
Hilda HernandezDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, United States.
Jürgen CoxDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Alma L BurlingameDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, United States.
Jeffrey L BrodskyDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, United States.
Adam FrostDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.ORCID https://orcid.org/0000-0003-2231-2577
Georg Hh BornerDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID https://orcid.org/0000-0002-3166-3435
Jonathan S WeissmanDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States.ORCID http://orcid.org/0000-0003-2445-670X
University of California, San Francisco · USMax Planck Institute of Biochemistry · DEUniversity of Pittsburgh · USHoward Hughes Medical Institute · US

Funding

Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
ER Associated Degradation of Membrane Proteins in YeastR01GM075061 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BRODSKY, JEFFREY L. · 2006 to 2019
$3.2M
Toward Atomic Resolution of Membranes and Membrane-Associated MachinesDP2GM110772 · NIGMS · UNIVERSITY OF UTAH · PI FROST, ADAM · 2013 to 2013
$2.2M
Human Gene Knockdowns that May Extend LifespanR01AG041826 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WEISSMAN, JONATHAN S. · 2012 to 2016
$1.6M
Purchase of Q-Exactive Mass SpectrometerS10OD016229 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2013 to 2013
$507k
European Research Council ERC2012-SyG_318987-ToPAGHoward Hughes Medical Institute Faculty Scholar GrantHoward Hughes Medical Institute Investigator ProgramNIA NIH HHS R01 AG041826NIGMS NIH HHS DP2 GM110772NIGMS NIH HHS P41 GM103481NIGMS NIH HHS R01 GM075061NIH HHS 1DP2GM110772-01NIH HHS 1S10OD16229NIH HHS 8P41GM103481NIH HHS AG041826NIH HHS GM075061NIH HHS S10 OD016229
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) supports biosynthesis of proteins with diverse transmembrane domain (TMD) lengths and hydrophobicity. Features in transmembrane domains such as charged residues in ion channels are often functionally important, but could pose a challenge during cotranslational membrane insertion and folding. Our systematic proteomic approaches in both yeast and human cells revealed that the ER membrane protein complex (EMC) binds to and promotes the biogenesis of a range of multipass transmembrane proteins, with a particular enrichment for transporters. Proximity-specific ribosome profiling demonstrates that the EMC engages clients cotranslationally and immediately following clusters of TMDs enriched for charged residues. The EMC can remain associated after completion of translation, which both protects clients from premature degradation and allows recruitment of substrate-specific and general chaperones. Thus, the EMC broadly enables the biogenesis of multipass transmembrane proteins containing destabilizing features, thereby mitigating the trade-off between function and stability.

Indexed as

Protein BiosynthesisEndoplasmic ReticulumHumansMembrane ProteinsMolecular ChaperonesMultiprotein ComplexesProtein TransportProteomicsRibosomesSaccharomyces cerevisiaeMembrane ProteinsMolecular ChaperonesMultiprotein Complexescell biologyEMCendoplasmic reticulumhumanion channeltransmembranetransporter

Identifiers

PMID29809151
PMCPMC5995541
OpenAlexW2807099454

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.