ArticleNature2016
Cotranslational signal-independent SRP preloading during membrane targeting.
Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 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
101 citing papers in PubMed.
- Ribosome stalling position, spacing, and A-site occupancy impact translation and cotranslational mRNA decay in plants.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Co-translational protein targeting to mitochondria in the context of co-translational protein maturation.Protein science : a publication of the Protein Society · 2026Review
- SRP orchestrates protein biogenesis beyond initial ER membrane targeting.Nature communications · 2026Article
- Article
- A delayed translocation into the endoplasmic reticulum controls the post-translational modifications of PD-L1.Nature communications · 2026Article
- NAC promotes co-translational protein folding at the ribosomal tunnel exit.Molecular cell · 2026Article
- U2AF regulates the translation and localization of nuclear-encoded mitochondrial mRNAs.Molecular cell · 2026Article
- Article
- The endoplasmic reticulum in mitochondrial protein targeting: A neuronal perspective on organelle crosstalk.Protein science : a publication of the Protein Society · 2026Review
- Sec61β maintains cytoplasmic proteostasis via ARIH1-mediated translational repression upon ER stress.EMBO reports · 2026Article
- Structural basis of co-translational N-myristoylation in humans.Nature communications · 2026Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- Rules of Engagement for Components of Membrane Protein Biogenesis at the Human Endoplasmic Reticulum.International journal of molecular sciences · 2025Review
- A simple, fast, and cost-efficient protocol for ultra-sensitive ribosome profiling.Nucleic acids research · 2025Article
- Knowledge Discovery in Databases of Proteomics by Systems Modeling in Translational Research on Pancreatic Cancer.Proteomes · 2025Article
- Mechanism of chaperone recruitment and retention on mitochondrial precursors.Molecular biology of the cell · 2025Article
- 7SL RNA and signal recognition particle orchestrate a global cellular response to acute thermal stress.Nature communications · 2025Article
- A machine learning approach uncovers principles and determinants of eukaryotic ribosome pausing.Science advances · 2024Article
- A unifying model for membrane protein biogenesis.Nature structural & molecular biology · 2024Review
- The Effects of Codon Usage on Protein Structure and Folding.Annual review of biophysics · 2024Review
41 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Ribosome-associated factors must properly decode the limited information available in nascent polypeptides to direct them to their correct cellular fate. It is unclear how the low complexity information exposed by the nascent chain suffices for accurate recognition by the many factors competing for the limited surface near the ribosomal exit site. Questions remain even for the well-studied cotranslational targeting cycle to the endoplasmic reticulum, involving recognition of linear hydrophobic signal sequences or transmembrane domains by the signal recognition particle (SRP). Notably, the SRP has low abundance relative to the large number of ribosome-nascent-chain complexes (RNCs), yet it accurately selects those destined for the endoplasmic reticulum. Despite their overlapping specificities, the SRP and the cotranslationally acting Hsp70 display precise mutually exclusive selectivity in vivo for their cognate RNCs. To understand cotranslational nascent chain recognition in vivo, here we investigate the cotranslational membrane-targeting cycle using ribosome profiling in yeast cells coupled with biochemical fractionation of ribosome populations. We show that the SRP preferentially binds secretory RNCs before their targeting signals are translated. Non-coding mRNA elements can promote this signal-independent pre-recruitment of SRP. Our study defines the complex kinetic interaction between elongation in the cytosol and determinants in the polypeptide and mRNA that modulate SRP–substrate selection and membrane targeting.
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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.