ArticleScience (New York, N.Y.)2022
Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting.
Article in Science (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 100 citations in OpenAlex.
- A human cell-free translation screen identifies the NT-2 mycotoxin as a ribosomal inhibitor that binds the peptidyl transferase center.Communications biology · 2026Article
- GTPase cycle and ER membrane regulate cargo handover during cotranslational protein targeting.Science advances · 2026Article
- HSP47 in Mitochondria: Roles in Apoptosis, Signal Transduction, and Protein and Virus Transportation.Cells · 2026Review
- Structural basis of cotranslational protein N-terminal acetylation by NatB in human cells.Nature communications · 2026Article
- The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.Chemical reviews · 2026Review
- Gene Therapy Tools for Diseases Caused by Mutations of the Mitochondrial Genome.International journal of molecular sciences · 2026Review
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- 'Candidatus Liberibacter asiaticus' Effector SDE525 hijacks NACα to Suppress Jasmonic Acid-Mediated Immunity in Citrus.Molecular plant pathology · 2026Article
- NAC promotes co-translational protein folding at the ribosomal tunnel exit.Molecular cell · 2026Article
- Article
- A molecular switch in NAC prevents mitochondrial protein mistargeting by SRP.Nature communications · 2026Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2026Article
- NAA40 and NAC cooperate in co-translational histone acetylation in humans.Nature communications · 2026Article
- Structural basis of co-translational N-myristoylation in humans.Nature communications · 2026Article
- NatA engages in multi-factor complexes at the ribosomal polypeptide tunnel exit.Nature communications · 2026Article
- Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD.Science advances · 2025Article
- Temporal Regulation of Signal Recognition Particle During Translation.Journal of molecular biology · 2025Article
- Visualizing the translation landscape in human cells at high resolution.Nature communications · 2025Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking.Nature structural & molecular biology · 2025Article
6 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 4 countries.
Funding
Abstract
The nascent polypeptide-associated complex (NAC) interacts with newly synthesized proteins at the ribosomal tunnel exit and competes with the signal recognition particle (SRP) to prevent mistargeting of cytosolic and mitochondrial polypeptides to the endoplasmic reticulum (ER). How NAC antagonizes SRP and how this is overcome by ER targeting signals are unknown. Here, we found that NAC uses two domains with opposing effects to control SRP access. The core globular domain prevented SRP from binding to signal-less ribosomes, whereas a flexibly attached domain transiently captured SRP to permit scanning of nascent chains. The emergence of an ER-targeting signal destabilized NAC's globular domain and facilitated SRP access to the nascent chain. These findings elucidate how NAC hands over the signal sequence to SRP and imparts specificity of protein localization.
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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.