ArticleNucleic acids research2014
Direct binding of the Alu binding protein dimer SRP9/14 to 40S ribosomal subunits promotes stress granule formation and is regulated by Alu RNA.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 43 citations in OpenAlex.
- Reading the SINEs - functionality in noncoding RNA 'cheap genes'.RNA biology · 2026Review
- A B1 SINE element within the mouseScience advances · 2026Article
- Context-dependent release of HMGB1: cell death mode, cell type and LPS stress drive monomer and heterocomplex formation.Molecular medicine (Cambridge, Mass.) · 2026Article
- Translational regulation in stress biology.Nature cell biology · 2025Review
- 7SL RNA and signal recognition particle orchestrate a global cellular response to acute thermal stress.Nature communications · 2025Article
- lncRNA BC200 is processed into a stable Alu monomer.RNA (New York, N.Y.) · 2024Article
- Expression of signal recognition particle 14 in hepatocellular carcinoma and its relationship with disease progression and patient survival.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2024Article
- Significance of signal recognition particle 9 nuclear translocation: Implications for pancreatic cancer prognosis and functionality.International journal of oncology · 2024Article
- The role of SRP9/SRP14 in regulating Alu RNA.RNA biology · 2024Review
- Retrotransposon life cycle and its impacts on cellular responses.RNA biology · 2024Review
- Alu RNA fold links splicing with signal recognition particle proteins.Nucleic acids research · 2023Article
- Nuclear SRP9/SRP14 heterodimer transcriptionally regulates 7SL and BC200 RNA expression.RNA (New York, N.Y.) · 2023Article
- Alu antisense RNA ameliorates methylglyoxal-induced human lens epithelial cell apoptosis by enhancing antioxidant defense.International journal of ophthalmology · 2023Article
- DAB2IP down-regulates HSP90AA1 to inhibit the malignant biological behaviors of colorectal cancer.BMC cancer · 2022Article
- Blood Transcriptome Analysis of Septic Patients Reveals a Long Non-CodingNon-coding RNA · 2022Article
- Signal Recognition Particle in Human Diseases.Frontiers in genetics · 2022Article
- Biology of PEST-Containing Nuclear Protein: A Potential Molecular Target for Cancer Research.Frontiers in oncology · 2022Review
- Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation.Communications biology · 2021Article
- Noncanonical Functions and Cellular Dynamics of the Mammalian Signal Recognition Particle Components.Frontiers in molecular biosciences · 2021Review
- ALU non-B-DNA conformations, flipons, binary codes and evolution.Royal Society open science · 2020Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Stress granules (SGs) are formed in response to stress, contain mRNAs, 40S ribosomal subunits, initiation factors, RNA-binding and signaling proteins, and promote cell survival. Our study describes a novel function of the protein heterodimer SRP9/14 and Alu RNA in SG formation and disassembly. In human cells, SRP9/14 exists assembled into SRP, bound to Alu RNA and as a free protein. SRP9/14, but not SRP, localizes to SGs following arsenite or hippuristanol treatment. Depletion of the protein decreases SG size and the number of SG-positive cells. Localization and function of SRP9/14 in SGs depend primarily on its ability to bind directly to the 40S subunit. Binding of SRP9/14 to 40S and Alu RNA is mutually exclusive indicating that the protein alone is bound to 40S in SGs and that Alu RNA might competitively regulate 40S binding. Indeed, by changing the effective Alu RNA concentration in the cell or by expressing an Alu RNA binding-defective protein we were able to influence SG formation and disassembly. Our findings suggest a model in which SRP9/14 binding to 40S promotes SG formation whereas the increase in cytoplasmic Alu RNA following stress promotes disassembly of SGs by disengaging SRP9/14 from 40S.
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Registered trials
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