ArticleNucleic acids research2014
Homodimerization of RBPMS2 through a new RRM-interaction motif is necessary to control smooth muscle plasticity.
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 24 papers.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Comprehensive analyses of biological function and tumor microenvironment with cuproptosis regulators and construction of a cuproptosis-related scoring system in thyroid cancer based on bioinformatics and experimental validation.Frontiers in genetics · 2026Article
- Obesity induces phenotypic switching of gastric smooth muscle cells through the activation of the PPARD/PDK4/ANGPTL4 pathway.Journal of biomedical science · 2025Article
- Elongation factor 2 in cancer: a promising therapeutic target in protein translation.Cellular & molecular biology letters · 2024Review
- Cell-type specific regulator RBPMS switches alternative splicing via higher-order oligomerization and heterotypic interactions with other splicing regulators.Nucleic acids research · 2023Article
- eEF2 improves dense connective tissue repair and healing outcome by regulating cellular death, autophagy, apoptosis, proliferation and migration.Cellular and molecular life sciences : CMLS · 2023Article
- Exploiting Multi-Omics Profiling and Systems Biology to Investigate Functions of TOMM34.Biology · 2023Article
- Phosphorylation of the smooth muscle master splicing regulator RBPMS regulates its splicing activity.Nucleic acids research · 2022Article
- Prognostic value of noggin protein expression in patients with resected gastric cancer.BMC cancer · 2021Article
- Phenotypic switch of smooth muscle cells in paediatric chronic intestinal pseudo-obstruction syndrome.Journal of cellular and molecular medicine · 2021Article
- An Innovative Prognostic Model Based on Four Genes in Asian Patient with Gastric Cancer.Cancer research and treatment · 2021Article
- Infantile fibrosarcoma-like tumor driven by novelCold Spring Harbor molecular case studies · 2020Article
- Loss ofDevelopment (Cambridge, England) · 2020Article
- Exploring the Activities of RBPMS Proteins in Myocardial Biology.Pediatric cardiology · 2019Review
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- 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
- Integrative Genomics Analysis Unravels Tissue-Specific Pathways, Networks, and Key Regulators of Blood Pressure Regulation.Frontiers in cardiovascular medicine · 2019Article
- rbpms2 functions in Balbiani body architecture and ovary fate.PLoS genetics · 2018Article
- Chick midgut morphogenesis.The International journal of developmental biology · 2018Review
- Conserved binding of GCAC motifs by MEC-8, couch potato, and the RBPMS protein family.RNA (New York, N.Y.) · 2017Article
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In vertebrates, smooth muscle cells (SMCs) can reversibly switch between contractile and proliferative phenotypes. This involves various molecular mechanisms to reactivate developmental signaling pathways and induce cell dedifferentiation. The protein RBPMS2 regulates early development and plasticity of digestive SMCs by inhibiting the bone morphogenetic protein pathway through its interaction with NOGGIN mRNA. RBPMS2 contains only one RNA recognition motif (RRM) while this motif is often repeated in tandem or associated with other functional domains in RRM-containing proteins. Herein, we show using an extensive combination of structure/function analyses that RBPMS2 homodimerizes through a particular sequence motif (D-x-K-x-R-E-L-Y-L-L-F: residues 39-51) located in its RRM domain. We also show that this specific motif is conserved among its homologs and paralogs in vertebrates and in its insect and worm orthologs (CPO and MEC-8, respectively) suggesting a conserved molecular mechanism of action. Inhibition of the dimerization process through targeting a conserved leucine inside of this motif abolishes the capacity of RBPMS2 to interact with the translational elongation eEF2 protein, to upregulate NOGGIN mRNA in vivo and to drive SMC dedifferentiation. Our study demonstrates that RBPMS2 possesses an RRM domain harboring both RNA-binding and protein-binding properties and that the newly identified RRM-homodimerization motif is crucial for the function of RBPMS2 at the cell and tissue levels.
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