ArticleQuarterly reviews of biophysics2016
Structural basis underlying CAC RNA recognition by the RRM domain of dimeric RNA-binding protein RBPMS.
Article in Quarterly reviews of biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 58 citations in OpenAlex.
- The role of lncRNA HUPCOS in androgen metabolism and follicle growth arrest in polycystic ovary syndrome.Cell biology and toxicology · 2025Article
- The RNA-binding protein RBPMS inhibits smooth muscle cell-driven vascular remodeling in atherosclerosis and vascular injury.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- RBPMS regulates cardiomyocyte contraction and cardiac function through RNA alternative splicing.Cardiovascular research · 2024Article
- Cell-type specific regulator RBPMS switches alternative splicing via higher-order oligomerization and heterotypic interactions with other splicing regulators.Nucleic acids research · 2023Article
- Article
- mRNA translational specialization by RBPMS presets the competence for cardiac commitment in hESCs.Science advances · 2023Article
- Insight into the Structural Basis for Dual Nucleic Acid-Recognition by the Scaffold Attachment Factor B2 Protein.International journal of molecular sciences · 2023Article
- Phosphorylation of the smooth muscle master splicing regulator RBPMS regulates its splicing activity.Nucleic acids research · 2022Article
- Comprehensive landscape of the functions and prognostic value of RNA binding proteins in uterine corpus endometrial carcinoma.Frontiers in molecular biosciences · 2022Article
- A Novel Family of RNA-Binding Proteins Regulate Polysaccharide Metabolism inJournal of bacteriology · 2021Article
- Structural basis of PETISCO complex assembly during piRNA biogenesis inGenes & development · 2021Article
- Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?Cell death & disease · 2021Review
- Infantile fibrosarcoma-like tumor driven by novelCold Spring Harbor molecular case studies · 2020Article
- Posttranscriptional Gene Regulatory Networks in Chronic Airway Inflammatory Diseases:Frontiers in immunology · 2020Article
- Exploring the Activities of RBPMS Proteins in Myocardial Biology.Pediatric cardiology · 2019Review
- Article
- Molecular basis for AU-rich element recognition and dimerization by the HuR C-terminal RRM.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- rbpms2 functions in Balbiani body architecture and ovary fate.PLoS genetics · 2018Article
- Article
- Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate.Nucleic acids research · 2017Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
RNA-binding protein with multiple splicing (designated RBPMS) is a higher vertebrate mRNA-binding protein containing a single RNA recognition motif (RRM). RBPMS has been shown to be involved in mRNA transport, localization and stability, with key roles in axon guidance, smooth muscle plasticity, as well as regulation of cancer cell proliferation and migration. We report on structure-function studies of the RRM domain of RBPMS bound to a CAC-containing single-stranded RNA. These results provide insights into potential topologies of complexes formed by the RBPMS RRM domain and the tandem CAC repeat binding sites as detected by photoactivatable-ribonucleoside-enhanced crosslinking and immunoprecipitation. These studies establish that the RRM domain of RBPMS forms a symmetrical dimer in the free state, with each monomer binding sequence-specifically to all three nucleotides of a CAC segment in the RNA bound state. Structure-guided mutations within the dimerization and RNA-binding interfaces of RBPMS RRM on RNA complex formation resulted in both disruption of dimerization and a decrease in RNA-binding affinity as observed by size exclusion chromatography and isothermal titration calorimetry. As anticipated from biochemical binding studies, over-expression of dimerization or RNA-binding mutants of Flag-HA-tagged RBPMS were no longer able to track with stress granules in HEK293 cells, thereby documenting the deleterious effects of such mutations in vivo.
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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.