ArticleProceedings of the National Academy of Sciences of the United States of America2005
Cold stress-induced protein Rbm3 binds 60S ribosomal subunits, alters microRNA levels, and enhances global protein synthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.
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Who cites it
118 citing papers in PubMed, 247 citations in OpenAlex.
- RMRP mediates neuroprotection as a downstream effector of RBM3 in human neuroblastoma SH-SY5Y cells.Molecular genetics and genomics : MGG · 2026Article
- Augmenting the Endogenous RBM3 Response Protects Against Burn-Induced Acute Kidney Injury by Enhancing Macrophage-Mediated Resolution of Inflammation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Fever Inspiration: Precision Engineering for Safe and Systemic Immunotherapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Molecular mediators of cold adaptation in mammalian cells.Communications biology · 2025Review
- A review on gut microbiota and miRNA crosstalk: implications for Alzheimer's disease.GeroScience · 2025Review
- Therapeutic modulation of protein RBM3 for ischemic stroke treatment.Frontiers in pharmacology · 2025Review
- Cold-shock proteome of myoblasts reveals role of RBM3 in promotion of mitochondrial metabolism and myoblast differentiation.Communications biology · 2024Article
- Bmal1 integrates circadian function and temperature sensing in the suprachiasmatic nucleus.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Transport of CLCA2 to the nucleus by extracellular vesicles controls keratinocyte survival and migration.Journal of extracellular vesicles · 2024Article
- Bovine oviductal organoids: a multi-omics approach to capture the cellular and extracellular molecular response of the oviduct to heat stress.BMC genomics · 2023Article
- Hypothermia increases cold-inducible protein expression and improves cerebellar-dependent learning after hypoxia ischemia in the neonatal rat.Pediatric research · 2023Article
- Integrated Analysis of DNA Methylome and Transcriptome Reveals Epigenetic Regulation of Cold Tolerance inInternational journal of molecular sciences · 2023Article
- Senescent immune cells accumulation promotes brown adipose tissue dysfunction during aging.Nature communications · 2023Article
- Review
- RNA-Binding Proteins in Bladder Cancer.Cancers · 2023Review
- The transcript interactome of skeletal muscle RNA binding protein motif 3 (RBM3).Physiological reports · 2023Article
- The DNA repair enzyme, aprataxin, plays a role in innate immune signaling.Frontiers in aging neuroscience · 2023Article
- Mild hypothermia ameliorates hepatic ischemia reperfusion injury by inducing RBM3 expression.Apoptosis : an international journal on programmed cell death · 2022Article
- Understanding the Function and Mechanism of Zebrafish Tmem39b in Regulating Cold Resistance.International journal of molecular sciences · 2022Article
- RNA-binding protein RBM3 intrinsically suppresses lung innate lymphoid cell activation and inflammation partially through CysLT1R.Nature communications · 2022Article
58 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The expression of Rbm3, a glycine-rich RNA-binding protein, is enhanced under conditions of mild hypothermia, and Rbm3 has been postulated to facilitate protein synthesis at colder temperatures. To investigate this possibility, Rbm3 was overexpressed as a c-Myc fusion protein in mouse neuroblastoma N2a cells. Cells expressing this fusion protein showed a 3-fold increase in protein synthesis at both 37 degrees C and 32 degrees C compared with control cells. Although polysome profiles of cells expressing the fusion protein and control cells were similar, several differences were noted, suggesting that Rbm3 might enhance the association of 40S and 60S ribosomal subunits at 32 degrees C. Studies to assess a direct interaction of Rbm3 with ribosomes showed that a fraction of Rbm3 was associated with 60S ribosomal subunits in an RNA-independent manner. It appeared unlikely that this association could explain the global enhancement of protein synthesis, however, because cells expressing the Rbm3 fusion protein showed no substantial increase in the size of their monosome and polysome peaks, suggesting that similar numbers of mRNAs were being translated at approximately the same rates. In contrast, a complex that sedimented between the top of the gradient and 40S subunits was less abundant in cells expressing recombinant Rbm3. Further analysis showed that the RNA component of this fraction was microRNA. We discuss the possibility that Rbm3 expression alters global protein synthesis by affecting microRNA levels and suggest that both Rbm3 and microRNAs are part of a homeostatic mechanism that regulates global levels of protein synthesis under normal and cold-stress conditions.
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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.