ArticleNature communications2025
SND3 is the membrane insertase within a distinct SEC61 translocon complex.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Cotranslational membrane protein biogenesis by an EMC-bound translocon.Nature structural & molecular biology · 2026Article
- Functional diversification across yeast lineages of the nucleus-vacuole junction forming protein Nvj1.bioRxiv : the preprint server for biology · 2026Article
- Pairwise transmembrane domain insertion during multipass protein biogenesis.Molecular cell · 2026Article
- Substrate-induced assembly and functional mechanism of the membrane protein insertase SecYEG-YidC.The EMBO journal · 2026Article
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- SARS-CoV-2 membrane protein biogenesis.bioRxiv : the preprint server for biology · 2026Article
- SND3 is the membrane insertase within a distinct SEC61 translocon complex.Nature communications · 2025Article
- Rules of Engagement for Components of Membrane Protein Biogenesis at the Human Endoplasmic Reticulum.International journal of molecular sciences · 2025Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
During the biogenesis of most eukaryotic integral membrane proteins (IMPs), transmembrane domains are inserted into the endoplasmic reticulum membrane by a dedicated insertase or the SEC61 translocon. The SRP-independent (SND) pathway is the least understood route into the membrane, despite catering for a broad range of IMP types. Here, we show that Chaetomium thermophilum SND3 is a membrane insertase with an atypical fold. We further present a cryo-electron microscopy structure of a ribosome-associated SND3 translocon complex involved in co-translational IMP insertion. The structure reveals that the SND3 translocon additionally comprises the complete SEC61 translocon, CCDC47 and TRAPɑ. Here, the SEC61β N-terminus works together with CCDC47 to prevent substrate access to the translocon. Instead, molecular dynamics simulations show that SND3 disrupts the lipid bilayer to promote IMP insertion via its membrane-embedded hydrophilic groove. Structural and sequence comparisons indicate that the SND3 translocon is a distinct multipass translocon in fungi, euglenozoan parasites and other eukaryotic taxa.
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Registered trials
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