ArticleBMB reports2018
The multifunctional RNA-binding protein hnRNPK is critical for the proliferation and differentiation of myoblasts.
Article in BMB reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Metabolic signatures of triple-negative breast cancer.Molecular biology reports · 2026Review
- A Modular and Programmable Cas13d Platform for RNA Single Nucleotide Variant Detection.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- RNA-binding protein hnRNPK: a multifunctional regulator of skeletal muscle biology and disease.Biochemical Society transactions · 2026Review
- TDP43 and hnRNP K Regulate Alternative Splicing of DNAJC5.Cell biology international · 2026Article
- RPS27L Enhances Myogenesis and Muscle Mass by Targeting IGF1 Through Liquid-Liquid Phase Separation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The paradox of hnRNPK: both absence and excess impair skeletal muscle function in mice.Skeletal muscle · 2025Article
- Insights into the role of hnRNPK in spermatogenesis via the piRNA pathway.Scientific reports · 2025Article
- Article
- hnRNPK-derived cell-penetratingpeptide inhibits cancer cell survival.Molecular therapy oncolytics · 2021Article
- RNA-Binding Proteins in the Post-transcriptional Control of Skeletal Muscle Development, Regeneration and Disease.Frontiers in cell and developmental biology · 2021Review
- Stress-Induced Accumulation of HnRNP K into Stress Granules.Journal of cancer science and clinical therapeutics · 2021Article
- hnRNPK knockdown alleviates NLRP3 inflammasome priming by repressing FLIP expression in Raw264.7 macrophages.Redox report : communications in free radical research · 2020Article
- Review
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Authors and funding
7 authors at 1 institution in 1 country.
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Abstract
HnRNPK is a multifunctional protein that participates in chromatin remodeling, transcription, RNA splicing, mRNA stability and translation. Here, we uncovered the function of hnRNPK in regulating the proliferation and differentiation of myoblasts. hnRNPK was mutated in the C2C12 myoblast cell line using the CRISPR/Cas9 system. A decreased proliferation rate was observed in hnRNPK-mutated cells, suggesting an impaired proliferation phenotype. Furthermore, increased G2/M phase, decreased S phase and increased sub-G1 phase cells were detected in the hnRNPK-mutated cell lines. The expression analysis of key cell cycle regulators indicated mRNA of Cyclin A2 was significantly increased in the mutant myoblasts compared to the control cells, while Cyclin B1, Cdc25b and Cdc25c were decreased sharply. In addition to the myoblast proliferation defect, the mutant cells exhibited defect in myotube formation. The myotube formation marker, myosin heavy chain (MHC), was decreased sharply in hnRNPK-mutated cells compared to control myoblasts during differentiation. The deficiency in hnRNPK also resulted in the repression of Myog expression, a key myogenic regulator during differentiation. Together, our data demonstrate that hnRNPK is required for myoblast proliferation and differentiation and may be an essential regulator of myoblast function. [BMB Reports 2018; 51(7): 350-355].
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