RSK2 mediates muscle cell differentiation through regulation of NFAT3
Open accessAbstract
RSK2, an ERK downstream kinase, is a novel mediator of skeletal muscle cell differentiation through its regulation of NFAT3 activity. We found that the N-terminal (amino acids (aa) 1-68) and C-terminal (aa 416-674) kinase domains of RSK2 directly interacted with nuclear localization signal 1, the Ser/Pro repeat, and the polyproline domains (aa 261-365) of NFAT3. Upon A23187 stimulation, RSK2 induced nuclear localization of NFAT3. RSK2 phosphorylated NFAT3 in vitro (Km=3.559 microM), and activation of NFAT3 by RSK2 enhanced the promoter activity of NFAT3 downstream target genes in vivo. Furthermore, nuclear accumulation of NFAT3 was attenuated markedly in RSK2-/- cells compared with wild-type RSK2+/+ cells. Notably, RSK2 and NFAT3 induced a significant differentiation of C2C12 myoblasts to multinucleated myotubes. Multinucleated myotube differentiation was inhibited by small interfering RNA against RSK2, ERK1/2, or NFAT3. These results demonstrate that RSK2 is an important kinase for NFAT3 in mediating myotube differentiation.
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During late stages of differentiation, ERK1/2 becomes phosphorylated, promoting fusion and formation of myotubes.
“In contrast to this inhibitory effect during the early stages of differentiation ERK1/2 becomes phosphorylated during the late stages of differentiation promoting the fusion and formation of myotubes [129,130].”
From Potential Roles of n-3 PUFAs during Skeletal Muscle Growth and Regeneration (2018) · cites this paper as [129]
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References 54 · Cited by 85
- Authors
- Cho, Y.-Y., Yao, K., Bode, A. M., Bergen, H. R., Madden, B. J., Oh, S.-M., Ermakova, S., Kang, B. S., Choi, H. S., Shim, J.-H., & Dong, Z.
- Affiliations
- University of Minnesota (US)
- Mayo Clinic (US)
- Corresponding author
- Dong, Zigang
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-03
- Volume
- 282
- Issue
- 11
- Pages
- 8380-8392
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2824544
- OpenAlex
- W2097041188
- Cited by
- 85
- References
- 54
- Citations by year
- 2026: 3 · 2025: 2 · 2023: 7 · 2022: 11 · 2021: 2 · 2020: 2 · 2019: 4 · 2018: 4 · 2017: 4 · 2016: 4 · 2015: 6 · 2014: 3 · 2013: 6 · 2012: 6
- FWCI
- 2.25
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (R01CA077646, CA 27502, P01CA088961, R01CA081064, CA-81064, CA 88961, R37CA081064, CA 77646, P01CA027502)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- RSK2, NFATc3, skeletal muscle differentiation, myotube differentiation, protein phosphorylation, nuclear localization, C2C12 myoblasts, nuclear localization signal, ERK1/2
- MeSH terms
- Amino Acid Sequence, Animals, Cell Differentiation, Enzyme Inhibitors, Gene Expression Regulation, Humans, Molecular Sequence Data, Muscles, Protein Binding, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Ribosomal Protein S6 Kinases, 90-kDa, NFATC Transcription Factors, Mice
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