RNA‐binding proteins Rbm38 and Rbm24 regulate myogenic differentiation via p21‐dependent and ‐independent regulatory pathways
Abstract
Skeletal muscle differentiation entails organized sequential events, including cell cycle arrest of proliferating myoblast cells and cell fusion, which lead to the formation of multinucleated myotubes. This process involves both transcriptional and post‐transcriptional regulation of the gene expression of myogenic proteins, as well as cell‐cycle related proteins. RNA‐binding proteins bind to specific sequences of target RNA and regulate gene expression in a post‐transcriptional manner. However, few tissue‐specific RNA binding proteins have been identified. Herein, we report that the RNA binding proteins Rbm24 and Rbm38 were found to be preferentially expressed in muscle during differentiation in vitro . Further, knockdown of either by RNA interference suppressed cell‐cycle arrest and delayed myogenic differentiation in C2C12 cells. In contrast, over‐expression of Rbm24 or Rbm38 induced cell cycle arrest, and then had a positive effect on myogenic differentiation. Immunoprecipitation‐RT‐PCR analysis using tagged Rbm proteins indicated that Rbm38 binds to the p21 transcript in vivo . Consistent with this, differentiation of Rbm38 knockdown cells was rescued by over‐expression of p21. Together, our results suggest that Rbm38 plays a crucial role in cell cycle arrest and myogenic differentiation via its binding to p21.
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The SUP12, RBM24, and RBM38 proteins are regulators of muscle development in nematode, mouse, and human, indicating biochemical and functional conservation.
“These nematode, mouse and human proteins are regulators of muscle development15,16, indicating both biochemical and functional conservation.”
From A compendium of RNA-binding motifs for decoding gene regulation (2013) · cites this paper as [15]
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ResultRNA‐binding motif protein 24 regulates myogenin expression and promotes myogenic differentiation
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“show enriched expression of Rbm38 in heart- and skeletal muscle, while others have shown specificity of Rbm38 in erythrocytes [15, 16].”
BackgroundResultRbm24a Is Necessary for Hair Cell Development Through Regulating mRNA Stability in Zebrafish
Zhang, Y., Wang, Y., Yao, X., Wang, C., Chen, F., Liu, D., Shao, M., & Xu, Z. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.604026 · Cited by 16 · see citing works
“Rbm24 knockdown in C2C12 cells, Xenopus, or chick somatic myogenic progenitor cells affects myogenic differentiation (Miyamoto et al., 2009; Li et al., 2010; Grifone et al., 2014).”
BackgroundThe Complex Landscape of PTEN mRNA RegulationPreprint
Sellars, E., Gabra, M., & Salmena, L. (2019) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a036236 · Cited by 16 · see citing works
Ding, Z., Yang, H., Xia, T., Wang, B., & Ding, Q. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2237 · Cited by 15 · see citing works
“It can also bind and stabilize the mRNA of the CDK inhibitor, p21, thereby inducing cell cycle arrest in the G1 phase (7,8).”
Sonnenschein, K., Fiedler, J., Pfanne, A., Just, A., Mitzka, S., Geffers, R., Pich, A., Bauersachs, J. K., & Thum, T. (2019) · Cardiovascular Research · doi:10.1093/cvr/cvz063 · Cited by 14 · see citing works
Yan, W., Zhang, Y., & Chen, X. (2017) · Oncotarget · doi:10.18632/oncotarget.18463 · Cited by 14 · see citing works
“For example, RBM38, a RNAbinding protein and a target of the p53 family, is able to stabilize p21 transcript and consequently suppresses cell growth [19-22].”
Backgrounddos Reis, E. P., Paixão, D. M., Brustolini, O. J. B., Silva, F. F. E., da Silva, W., Araújo, F. M. G., Salim, A. C. M., Oliveira, G., & Guimarães, S. E. F. (2016) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2015-0295 · Cited by 13 · see citing works
“RBM24 protein interacts with MYOG mRNA to regulate the stability and expression of the latter through a post-transcriptional regulatory pathway (Jin et al., 2010), but can also promote myogenic differentiation by modulating the cell cycle (Miyamoto et al., 2009).”
BackgroundRNA binding Motif protein-38 regulates myocardial hypertrophy in LXR-α-dependent lipogenesis pathway
Li, Y., Shi, Y., He, Y., Li, X.-M., & Yang, J. (2021) · Bioengineered · doi:10.1080/21655979.2021.1977552 · Cited by 11 · see citing works
“For instance, it has been mentioned as a regulator of Fgfr2 splicing in epithelial cells [25]; it regulates RNA processes, including splicing, translation, stability, and the accessibility of microRNA to the specific mRNA target [26].”
BackgroundSun, W., Laubach, K., Lucchesi, C. A., Zhang, Y., Chen, M., Zhang, J., & Chen, X. (2021) · Genes & Development · doi:10.1101/gad.346148.120 · Cited by 11 · see citing works
“RBM38 has been implicated in multiple cellular processes, such as cell cycle arrest and differentiation, by regulating its downstream targets (Miyamoto et al. 2009; Zhang et al. 2010; Heinicke et al. 2013; Yin et al. 2013).”
Zhang, J., Kong, X., Sun, W., Wang, L., Shen, T., Chen, M., & Chen, X. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1008576 · Cited by 10 · see citing works
“Previous studies have suggested that RBM24 and RBM38 have distinct and overlapped biological functions (Miyamoto et al., 2009; Zhang et al., 2010; Xu et al., 2014; Zhang et al., 2018a; Shao et al., 2020a).”
BackgroundRNA-binding protein RBM38 acts as a tumor suppressor in gastric cancer.
Wang, P., Gu, J. H., Li, X., Wang, Q., & Ding, Y. (2017) · PubMed Central · Cited by 7 · see citing works
RBM12 regulates the progression of hepatocellular cancer via miR-497–5p/CPNE1 Axis
Gao, C., Zhu, R., Shen, J., Xu, T., She, Y., & Chen, Z. (2023) · Environmental Research · doi:10.1016/j.envres.2023.117203 · Cited by 5 · see citing works
Shi, D., Grifone, R., Zhang, X., & Li, H. (2024) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-024-09685-5 · Cited by 4 · see citing works
“In the myotome, it is still unclear how cytoplasmic Rbm24 functions to promote the differentiation of fate-com - mitted myoblasts, although it can regulate myogenic gene expression and cell cycle arrest in C2C12 cells (Jin et al. 2010; Miyamoto et al. 2009 ).”
Sun, W., Hu, Y., Xu, H., He, H., Han, C., Liu, H., Wang, J., & Li, L. (2016) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2016.03.008 · Cited by 3 · see citing works
Wang, H., Li, A., An, C., Che, S., Huang, R. S., Liu, S., & Zhuang, Z. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.144156 · Cited by 1 · see citing works
Zhang, X., Li, X., Liu, R., Wang, L., Wang, Y., Zhang, A., Yang, S., & Li, H. (2025) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjaf025 · Cited by 1 · see citing works
“Their expression patterns show remarkable similarity, which is consistent with their redundant functions (Miyamoto et al., 2009 ; Sun et al., 2016 ; van den Hoogenhof et al., 2017 ; Grifone et al., 2020 ).”
1H, 15N and 13C backbone and side chain resonance assignments of the RRM domain from human RBM24
Upadhyay, S. K., & Mackereth, C. D. (2016) · Biomolecular NMR Assignments · doi:10.1007/s12104-016-9674-y · Cited by 1 · see citing works
“Reduction in RBM24 levels was also marked by cell cycle arrest via several pathways including direct interaction with the p21 transcript (Miyamoto et al. 2009; Jiang et al. 2014) and other components of the p53 network (Jiang et al.”
BackgroundKoutsoulidou, A., Mastroyiannopoulos, N. P., & Phylactou, L. A. (2013) · Encyclopedia of Molecular Cell Biology and Molecular Medicine · doi:10.1002/3527600906.mcb.201200033
Evolutionary Conservation and Functional Diversification of the Rbm24/38 Family in Metazoans
Zhang, X., Zhang, A., Bai, Z., & Li, H. (2026) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.70054
“Subsequent investigations suggested that both Rbm38 and Rbm24 could be homologs of the nematode Sup-12 , raising the possibility that they are paralogs originating from an ancestral gene by gene duplication event (Grifone et al. 2020; Miyamoto et al. 2009; Ray et al. 2009; Heinicke et al. 2013).”
InfluentialThe Role of ERK5 in Cell Proliferation
Madrigal, D. P. (2013) · [Thesis]. Manchester, UK: The University of Manchester; 2013.
- Authors
- Miyamoto, S., Hidaka, K., Jin, D., & Morisaki, T.
- Affiliations
- National Cerebral and Cardiovascular Center (JP)
- The University of Osaka (JP)
- Corresponding author
- Morisaki, Takayuki
- ORCID
- Morisaki, Takayuki
- Venue
- Genes to Cells
- Publisher
- Wiley
- Published
- 2009-11
- Volume
- 14
- Issue
- 11
- Pages
- 1241-1252
- ISSN
- 1356-9597 (ISSN-L)
- 1365-2443
- OpenAlex
- W2125806220
- Cited by
- 64
- References
- 32
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 5 · 2020: 2 · 2019: 5 · 2018: 2 · 2017: 7 · 2016: 7 · 2015: 1 · 2014: 8 · 2013: 8 · 2012: 4
- FWCI
- 1.61
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Genes to Cells (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Science and Technology Corporation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- RBM38, RBM24, RNA-binding proteins, myogenesis, skeletal muscle differentiation, p21, cell cycle arrest, post-transcriptional regulation, C2C12 myoblasts, cell fusion
- MeSH terms
- Animals, Cell Differentiation, Cell Line, Fluorescent Antibody Technique, Gene Expression Regulation, Myocardium, Signal Transduction, Up-Regulation, RNA-Binding Proteins, Muscle, Skeletal, Gene Silencing, Mice, p21-Activated Kinases, Gene Knockdown Techniques
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