ArticleNature2014
Structures of the Sec61 complex engaged in nascent peptide translocation or membrane insertion.
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.
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Who cites it
126 citing papers in PubMed.
- Protein secretion routes in fungi are predicted by the length of the hydrophobic helix in the signal sequence.G3 (Bethesda, Md.) · 2026Article
- SRP orchestrates protein biogenesis beyond initial ER membrane targeting.Nature communications · 2026Article
- Identification of a Novel De Novo Heterozygous SEC61A1 Variant in a Patient With Severe Congenital Neutropenia.Molecular genetics & genomic medicine · 2026Article
- Article
- ATP13A1 engages SEC61 to facilitate substrate-specific translocation.Science advances · 2025Article
- Sequence-dependent scale for translocon-mediated insertion of interfacial helices in membranes.Science advances · 2025Article
- Toward Understanding the Mechanism of Client-Selective Small Molecule Inhibitors of the Sec61 Translocon.Journal of molecular recognition : JMR · 2025Review
- Role of Sec61α2 Translocon in Insulin Biosynthesis.Diabetes · 2024Article
- Redox regulation of UPR signalling and mitochondrial ER contact sites.Cellular and molecular life sciences : CMLS · 2024Review
- Cryo-EM structure of wheat ribosome reveals unique features of the plant ribosomes.Structure (London, England : 1993) · 2024Article
- SEC61 translocon subunit gamma enhances low-dose cisplatin-induced cancer-stem cell properties of head and neck squamous cell carcinoma via enhancing CaJournal of dental sciences · 2023Article
- Signal peptide mimicry primes Sec61 for client-selective inhibition.Nature chemical biology · 2023Article
- A common mechanism of Sec61 translocon inhibition by small molecules.Nature chemical biology · 2023Article
- Transgene-induced cell death following dengue-2 virus infection in Aedes aegypti.Scientific reports · 2023Article
- Structural basis of SecA-mediated protein translocation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023Review
- Predicting the Assembly of the Transmembrane Domains of Viral Channel Forming Proteins and Peptide Drug Screening Using a Docking Approach.Biomolecules · 2022Article
- Three-stage model of helical membrane protein folding: Role of membrane-water interface as the intermediate stage vestibule for TM helices during their in membrano assembly.Biochemical and biophysical research communications · 2022Article
- Phenylbutyrate rescues the transport defect of the Sec61α mutations V67G and T185A for renin.Life science alliance · 2022Article
- The ER membrane complex (EMC) can functionally replace the Oxa1 insertase in mitochondria.PLoS biology · 2022Article
66 more citing papers are in PubMed but not listed here.
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7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biogenesis of secretory as well as transmembrane proteins requires the activity of the universally conserved protein-conducting channel (PCC), the Sec61 complex (SecY complex in bacteria). In eukaryotic cells the PCC is located in the membrane of the endoplasmic reticulum where it can bind to translating ribosomes for co-translational protein transport. The Sec complex consists of three subunits (Sec61α, β and γ) and provides an aqueous environment for the translocation of hydrophilic peptides as well as a lateral opening in the Sec61α subunit that has been proposed to act as a gate for the membrane partitioning of hydrophobic domains. A plug helix and a so-called pore ring are believed to seal the PCC against ion flow and are proposed to rearrange for accommodation of translocating peptides. Several crystal and cryo-electron microscopy structures revealed different conformations of closed and partially open Sec61 and SecY complexes. However, in none of these samples has the translocation state been unambiguously defined biochemically. Here we present cryo-electron microscopy structures of ribosome-bound Sec61 complexes engaged in translocation or membrane insertion of nascent peptides. Our data show that a hydrophilic peptide can translocate through the Sec complex with an essentially closed lateral gate and an only slightly rearranged central channel. Membrane insertion of a hydrophobic domain seems to occur with the Sec complex opening the proposed lateral gate while rearranging the plug to maintain an ion permeability barrier. Taken together, we provide a structural model for the basic activities of the Sec61 complex as a protein-conducting channel.
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