ArticleProceedings of the National Academy of Sciences of the United States of America2018
Sequential activation of human signal recognition particle by the ribosome and signal sequence drives efficient protein targeting.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- GTPase cycle and ER membrane regulate cargo handover during cotranslational protein targeting.Science advances · 2026Article
- Etiopathogenesis of Immune-Mediated Necrotizing Myopathy: A Comprehensive Review of Recent Advances.CNS neuroscience & therapeutics · 2026Review
- A molecular switch in NAC prevents mitochondrial protein mistargeting by SRP.Nature communications · 2026Article
- Temporal Regulation of Signal Recognition Particle During Translation.Journal of molecular biology · 2025Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- Anti-signal recognition particle antibodies induce cardiac diastolic dysfunction via oxidative stress injury.Clinical & translational immunology · 2024Article
- Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023Review
- Cotranslational Mechanisms of Protein Biogenesis and Complex Assembly in Eukaryotes.Annual review of biomedical data science · 2022Review
- Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022Review
- Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting.Science (New York, N.Y.) · 2022Article
- Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.International journal of molecular sciences · 2021Review
- Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation.International journal of molecular sciences · 2021Review
- Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle.Cell reports · 2021Article
- Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.Science advances · 2021Article
- Ribosome-bound Get4/5 facilitates the capture of tail-anchored proteins by Sgt2 in yeast.Nature communications · 2021Article
- A ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex.Nature communications · 2020Article
- Distinct Functions of Acyl/Alkyl Dihydroxyacetonephosphate Reductase in Peroxisomes and Endoplasmic Reticulum.Frontiers in cell and developmental biology · 2020Article
- A molecular recognition feature mediates ribosome-induced SRP-receptor assembly during protein targeting.The Journal of cell biology · 2019Article
- Reconstitution of the human SRP system and quantitative and systematic analysis of its ribosome interactions.Nucleic acids research · 2019Article
- Hydrophobicity, rather than secondary structure, is essential for the SRP dependent targeting of GPR35 to the ER membrane.Journal of bioenergetics and biomembranes · 2019Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Signal recognition particle (SRP) is a universally conserved targeting machine that mediates the targeted delivery of ∼30% of the proteome. The molecular mechanism by which eukaryotic SRP achieves efficient and selective protein targeting remains elusive. Here, we describe quantitative analyses of completely reconstituted human SRP (hSRP) and SRP receptor (SR). Enzymatic and fluorescence analyses showed that the ribosome, together with a functional signal sequence on the nascent polypeptide, are required to activate SRP for rapid recruitment of the SR, thereby delivering translating ribosomes to the endoplasmic reticulum. Single-molecule fluorescence spectroscopy combined with cross-complementation analyses reveal a sequential mechanism of activation whereby the ribosome unlocks the hSRP from an autoinhibited state and primes SRP to sample a variety of conformations. The signal sequence further preorganizes the mammalian SRP into the optimal conformation for efficient recruitment of the SR. Finally, the use of a signal sequence to activate SRP for receptor recruitment is a universally conserved feature to enable efficient and selective protein targeting, and the eukaryote-specific components confer upon the mammalian SRP the ability to sense and respond to ribosomes.
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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.