ArticleThe Journal of cell biology2014
Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting.
Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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.
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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
26 citing papers in PubMed, 36 citations in OpenAlex.
- Review
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- Actin Binding to the BAR Domain and Arf GAP Activity of ASAP1 Coordinately Control Actin Stress Fibers and Focal Adhesions.Biology of the cell · 2025Article
- Unveiling Differential Responses of Granulocytes to Distinct Immunostimulants with Implications in Autoimmune Uveitis.Biomedicines · 2023Article
- Spatiotemporal kinetics of the SRP pathway in liveProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Two Signal Recognition Particle Sequences Are Present in the Amino-Terminal Domain of the C-Tailed Protein SciP.Journal of bacteriology · 2020Article
- Alcohol Use Disorders Are Associated With a Unique Impact on Airway Epithelial Cell Gene Expression.Alcoholism, clinical and experimental research · 2020Article
- Structural Basis of the Subcellular Topology Landscape ofFrontiers in microbiology · 2019Article
- Cotranslational protein targeting to the membrane: Nascent-chain transfer in a quaternary complex formed at the translocon.Scientific reports · 2018Article
- Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence.Nucleic acids research · 2017Article
- Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.Nature communications · 2017Article
- Anionic Phospholipids and the Albino3 Translocase Activate Signal Recognition Particle-Receptor Interaction during Light-harvesting Chlorophyll a/b-binding Protein Targeting.The Journal of biological chemistry · 2017Article
- Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017Review
- ATPase and GTPase Tangos Drive Intracellular Protein Transport.Trends in biochemical sciences · 2016Review
- Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon.Nature communications · 2016Article
- Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon.The Journal of cell biology · 2015Article
- Multiply labeling proteins for studies of folding and stability.Current opinion in chemical biology · 2015Review
- Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions.Nature structural & molecular biology · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Efficient and accurate protein localization is essential to cells and requires protein-targeting machineries to both effectively capture the cargo in the cytosol and productively unload the cargo at the membrane. To understand how these challenges are met, we followed the interaction of translating ribosomes during their targeting by the signal recognition particle (SRP) using a site-specific fluorescent probe in the nascent protein. We show that initial recruitment of SRP receptor (SR) selectively enhances the affinity of SRP for correct cargos, thus committing SRP-dependent substrates to the pathway. Real-time measurement of cargo transfer from the targeting to translocation machinery revealed multiple factors that drive this event, including GTPase rearrangement in the SRP-SR complex, stepwise displacement of SRP from the ribosome and signal sequence by SecYEG, and elongation of the nascent polypeptide. Our results elucidate how active and sequential regulation of the SRP-cargo interaction drives efficient and faithful protein 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.