ArticleNature communications2019
A network of chaperones prevents and detects failures in membrane protein lipid bilayer integration.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.
What it found
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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.
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.
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Who cites it
27 citing papers in PubMed, 43 citations in OpenAlex.
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- Roles of ER Membrane Protein Complex in Protein Biogenesis and Quality Control in the Lung and Beyond.Cell proliferation · 2026Review
- Membrane-embedded polar residues target membrane proteins for degradation by the quality control protease FtsH.Nature communications · 2026Article
- SARS-CoV-2 membrane protein biogenesis.bioRxiv : the preprint server for biology · 2026Article
- Targeted downmodulation of OXTR and Cx43 in the myometrium by SERTIs as a novel tocolytic strategy.Uterine research · 2026Article
- The EMC acts as a chaperone for membrane proteins.Nature communications · 2025Article
- Electrosome assembly: Structural insights from high voltage-activated calcium channel (CaV)-chaperone interactions.Biochemical Society transactions · 2025Review
- The Endoplasmic Reticulum Membrane Protein Complex Is Important for Deoxynivalenol Production and the Virulence ofJournal of fungi (Basel, Switzerland) · 2025Article
- Features of membrane protein sequence direct post-translational insertion.Nature communications · 2024Article
- TOLLIP acts as a cargo adaptor to promote lysosomal degradation of aberrant ER membrane proteins.The EMBO journal · 2023Article
- EMC chaperone-CaNature · 2023Article
- The Biogenesis of Multipass Membrane Proteins.Cold Spring Harbor perspectives in biology · 2023Review
- Intramembrane client recognition potentiates the chaperone functions of calnexin.The EMBO journal · 2022Article
- Calnexin reveals a sugar-free taste within the lipid bilayer.The EMBO journal · 2022Article
- The mechanisms of integral membrane protein biogenesis.Nature reviews. Molecular cell biology · 2022Review
- EMC is required for biogenesis of Xport-A, an essential chaperone of Rhodopsin-1 and the TRP channel.EMBO reports · 2022Article
- The Molecular Biodiversity of Protein Targeting and Protein Transport Related to the Endoplasmic Reticulum.International journal of molecular sciences · 2021Review
- The ER membrane protein complex subunit Emc3 controls angiogenesis via the FZD4/WNT signaling axis.Science China. Life sciences · 2021Article
- Revealing functional insights into ER proteostasis through proteomics and interactomics.Experimental cell research · 2021Review
- Ribosome-associated quality control of membrane proteins at the endoplasmic reticulum.Journal of cell science · 2020Review
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
Abstract
A fundamental step in membrane protein biogenesis is their integration into the lipid bilayer with a defined orientation of each transmembrane segment. Despite this, it remains unclear how cells detect and handle failures in this process. Here we show that single point mutations in the membrane protein connexin 32 (Cx32), which cause Charcot-Marie-Tooth disease, can cause failures in membrane integration. This leads to Cx32 transport defects and rapid degradation. Our data show that multiple chaperones detect and remedy this aberrant behavior: the ER-membrane complex (EMC) aids in membrane integration of low-hydrophobicity transmembrane segments. If they fail to integrate, these are recognized by the ER-lumenal chaperone BiP. Ultimately, the E3 ligase gp78 ubiquitinates Cx32 proteins, targeting them for degradation. Thus, cells use a coordinated system of chaperones for the complex task of membrane protein biogenesis, which can be compromised by single point mutations, causing human disease.
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Registered trials
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.