ArticleProceedings of the National Academy of Sciences of the United States of America2000
Signal recognition particle components in the nucleolus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
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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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Who cites it
97 citing papers in PubMed, 187 citations in OpenAlex.
- Signal recognition particle 14 binds to importin α in Plasmodium falciparum.Molecular biology reports · 2026Article
- Signaling to make human ribosomes: Connections between the cytoplasm and the nucleolus.Molecular cell · 2026Review
- Enhanced RNA quality control maintains long-term regenerative ability in planarians.Development (Cambridge, England) · 2025Article
- Alu RNA pseudoknot alterations influence SRP9/SRP14 association.RNA (New York, N.Y.) · 2025Article
- Nucleolar FRG2 lncRNAs inhibit rRNA transcription and cytoplasmic translation, linking FSHD to dysregulation of muscle-specific protein synthesis.Nucleic acids research · 2025Article
- 7SL RNA and signal recognition particle orchestrate a global cellular response to acute thermal stress.Nature communications · 2025Article
- Emergent microenvironments of nucleoli.Nucleus (Austin, Tex.) · 2024Review
- Single-cell laser emitting cytometry for label-free nucleolus fingerprinting.Nature communications · 2024Article
- The nucleolar phase of signal recognition particle assembly.Life science alliance · 2024Article
- Article
- The role of SRP9/SRP14 in regulating Alu RNA.RNA biology · 2024Review
- Beyond ribosome biogenesis: noncoding nucleolar RNAs in physiology and tumor biology.Nucleus (Austin, Tex.) · 2023Review
- Nuclear SRP9/SRP14 heterodimer transcriptionally regulates 7SL and BC200 RNA expression.RNA (New York, N.Y.) · 2023Article
- Deep genomic characterization highlights complexities and prognostic markers of pediatric acute myeloid leukemia.Communications biology · 2023Article
- Some natural compounds and their analogues having potent anti- SARS-CoV-2 and anti-proteases activities as lead molecules in drug discovery for COVID-19.European journal of medicinal chemistry reports · 2022Review
- Analysis of subcellular transcriptomes by RNA proximity labeling with Halo-seq.Nucleic acids research · 2022Article
- SRPassing Co-translational Targeting: The Role of the Signal Recognition Particle in Protein Targeting and mRNA Protection.International journal of molecular sciences · 2021Review
- RNA packaging into extracellular vesicles: An orchestra of RNA-binding proteins?Journal of extracellular vesicles · 2020Review
- Comparability of the small RNA secretome across human biofluids concomitantly collected from healthy adults.PloS one · 2020Article
- Scoring Functions for Protein-RNA Complex Structure Prediction: Advances, Applications, and Future Directions.Communications in information and systems · 2020Article
37 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
6 authors at 2 institutions in 1 country.
Funding
Abstract
The signal recognition particle (SRP) is a ribonucleoprotein composed of an Alu domain and an S domain. The S domain contains unique sequence SRP RNA and four SRP proteins: SRP19, SRP54, SRP68, and SRP72. SRP interacts with ribosomes to bring translating membrane and secreted proteins to the endoplasmic reticulum (ER) for proper processing. Additionally, SRP RNA is a member of a family of small nonribosomal RNAs found recently in the nucleolus, suggesting that the nucleolus is more plurifunctional than previously realized. It was therefore of interest to determine whether other SRP components localize to this intranuclear site. In transfected rat fibroblasts, green fluorescent protein fusions of SRP19, SRP68, and SRP72 localized to the nucleolus, as well as to the cytoplasm, as expected. SRP68 also accumulated in the ER, consistent with its affinity for the ER-bound SRP receptor. SRP54 was detected in the cytoplasm as a green fluorescent protein fusion and in immunofluorescence studies, but was not detected in the nucleolus. In situ hybridization experiments also revealed endogenous SRP RNA in the nucleolus. These results demonstrate that SRP RNA and three SRP proteins visit the nucleolus, suggesting that partial SRP assembly, or another unidentified activity of the SRP components, occurs at the nucleolus. SRP54 apparently interacts with nascent SRP beyond the nucleolus, consistent with in vitro reconstitution experiments showing that SRP19 must bind to SRP RNA before SRP54 binds. Our findings support the notion that the nucleolus is the site of assembly and/or interaction between the family of ribonucleoproteins involved in protein synthesis, in addition to ribosomes themselves.
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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.