ArticleNature communications2015
Structure of the native Sec61 protein-conducting channel.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.
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Who cites it
101 citing papers in PubMed.
- Mammalian MemPrep establishes the lipid composition of ER membranes in HEK293T cells.EMBO reports · 2026Article
- Global analysis of translocon remodeling during protein synthesis at the ER.Nature structural & molecular biology · 2025Article
- Rules of Engagement for Components of Membrane Protein Biogenesis at the Human Endoplasmic Reticulum.International journal of molecular sciences · 2025Review
- Effect of glycosylation on protein folding: From biological roles to chemical protein synthesis.iScience · 2025Review
- Cytoplasmic ribosomes on mitochondria alter the local membrane environment for protein import.The Journal of cell biology · 2025Article
- A subcellular map of translational machinery composition and regulation at the single-molecule level.Science (New York, N.Y.) · 2025Article
- Toward Understanding the Mechanism of Client-Selective Small Molecule Inhibitors of the Sec61 Translocon.Journal of molecular recognition : JMR · 2025Review
- Identification of Translocon-associated Protein Delta as An Oncogene in Human Colorectal Cancer Cells.Journal of cancer prevention · 2024Article
- Exploring the molecular composition of the multipass translocon in its native membrane environment.Life science alliance · 2024Article
- Cytoplasmic ribosomes on mitochondria alter the local membrane environment for protein import.bioRxiv : the preprint server for biology · 2024Article
- Article
- Comparative analysis of SEC61A1 mutant R236C in two patient-derived cellular platforms.Scientific reports · 2024Article
- Advances in the study of protein folding and endoplasmic reticulum-associated degradation in mammal cells.Journal of Zhejiang University. Science. B · 2024Review
- Molecular view of ER membrane remodeling by the Sec61/TRAP translocon.EMBO reports · 2023Article
- Quantitative Mass Spectrometry Characterizes Client Spectra of Components for Targeting of Membrane Proteins to and Their Insertion into the Membrane of the Human ER.International journal of molecular sciences · 2023Review
- Molecular basis of the TRAP complex function in ER protein biogenesis.Nature structural & molecular biology · 2023Article
- The Biogenesis of Multipass Membrane Proteins.Cold Spring Harbor perspectives in biology · 2023Review
- Mechanism of signal-anchor triage during early steps of membrane protein insertion.Molecular cell · 2023Article
- Structural insights into TRAP association with ribosome-Sec61 complex and translocon inhibition by a CADA derivative.Science advances · 2023Article
- The Endoplasmic Reticulum and the Fidelity of Nascent Protein Localization.Cold Spring Harbor perspectives in biology · 2023Review
41 more citing papers are in PubMed but not listed here.
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8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In mammalian cells, secretory and membrane proteins are translocated across or inserted into the endoplasmic reticulum (ER) membrane by the universally conserved protein-conducting channel Sec61, which has been structurally studied in isolated, detergent-solubilized states. Here we structurally and functionally characterize native, non-solubilized ribosome-Sec61 complexes on rough ER vesicles using cryo-electron tomography and ribosome profiling. Surprisingly, the 9-Å resolution subtomogram average reveals Sec61 in a laterally open conformation, even though the channel is not in the process of inserting membrane proteins into the lipid bilayer. In contrast to recent mechanistic models for polypeptide translocation and insertion, our results indicate that the laterally open conformation of Sec61 is the only conformation present in the ribosome-bound translocon complex, independent of its functional state. Consistent with earlier functional studies, our structure suggests that the ribosome alone, even without a nascent chain, is sufficient for lateral opening of Sec61 in a lipid environment.
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