Ontology highlight
ABSTRACT:
PROVIDER: PRJNA999372 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR25442714_1.fastq.gz | Fastqsanger.gz | |||
| SRR25442714_2.fastq.gz | Fastqsanger.gz | |||
| SRR25442715_1.fastq.gz | Fastqsanger.gz | |||
| SRR25442715_2.fastq.gz | Fastqsanger.gz | |||
| SRR25442716_1.fastq.gz | Fastqsanger.gz |
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Project description:The role of N6-methyladenosine (m6A) in muscle formation and maintenance remains incompletely understood, particularly with respect to the contribution of methyltransferase-like 3 (METTL3), the core component of the methyltransferase complex (MTC), to myogenesis. Here, we show the involvement of METTL3 in the m6A epitranscriptome during myogenesis. Our findings reveal a correlation between METTL3-regulated m6A modifications and myoblast fusion during differentiation and regeneration. We observed significant upregulation of METTL3 following injury and identified numerous alterations in myogenic pathways. Furthermore, we detected differential patterns of METTL3-regulated m6A modifications in genes during differentiation, with some genes exhibiting loss and others showing gain. Our study revealed that the fusion factors Mymx and Mymk are downstream elements of METTL3 involved in myogenesis, and both exhibit upregulated expression and m6A levels during myogenesis. Our findings provide valuable resources for elucidating the function and mechanism of METTL3-regulated m6A modifications in myogenesis, thereby revealing the regulatory role of METTL3 in myoblast fusion.
2025-09-03 | GSE293208 | GEO
Project description:The role of N6-methyladenosine (m6A) in muscle formation and maintenance remains incompletely understood, particularly with respect to the contribution of methyltransferase-like 3 (METTL3), the core component of the methyltransferase complex (MTC), to myogenesis. Here, we show the involvement of METTL3 in the m6A epitranscriptome during myogenesis. Our findings reveal a correlation between METTL3-regulated m6A modifications and myoblast fusion during differentiation and regeneration. We observed significant upregulation of METTL3 following injury and identified numerous alterations in myogenic pathways. Furthermore, we detected differential patterns of METTL3-regulated m6A modifications in genes during differentiation, with some genes exhibiting loss and others showing gain. Our study revealed that the fusion factors Mymx and Mymk are downstream elements of METTL3 involved in myogenesis, and both exhibit upregulated expression and m6A levels during myogenesis. Our findings provide valuable resources for elucidating the function and mechanism of METTL3-regulated m6A modifications in myogenesis, thereby revealing the regulatory role of METTL3 in myoblast fusion.
2025-09-03 | GSE293212 | GEO
Project description:Metabolic stress and changes in nutrient levels modulate many aspects of skeletal muscle function during aging and disease. Growth factors and cytokines secreted by skeletal muscle, known as myokines, are important signaling factors but it is largely unknown whether they modulate muscle growth and differentiation in response to nutrients. Here, we find that changes in glucose levels increase the activity of the glucose-responsive transcription factor MLX, which promotes and is necessary for myoblast fusion. MLX promotes myogenesis not via an adjustment of glucose metabolism but rather by inducing the expression of several myokines, including insulin like-growth factor-2 (IGF2), whereas RNAi and dominant-negative MLX reduce IGF2 expression and block myogenesis. This phenotype is rescued by conditioned media from control muscle cells and by recombinant IGF2, which activates the myogenic kinase Akt. Importantly, MLX null mice display decreased IGF2 induction and diminished muscle regeneration in response to injury, indicating that the myogenic function of MLX is conserved in vivo. Thus, glucose is a signaling molecule that regulates myogenesis and muscle regeneration via MLX/IGF2/Akt signaling.â??The data pproided are histome H4 acetlation data for MLX DN and MLX wt samples; 3 MLX DN H4 Ac Chip seq samples , 3 Inputs, 3 MLX WT H4 Ac samples and 3 WT inputs
2015-11-11 | E-GEOD-74678 | biostudies-arrayexpress
Project description:Upon muscle injury the high mobility group box 1 (HMGB1) protein is up-regulated and secreted to initiate reparative responses. Here we show that HMGB1 controls myogenesis both in vitro and in vivo, during development and after adult muscle injury. HMGB1 expression in muscle cells is regulated at the translational level: the miRNA miR-1192 inhibits HMGB1 translation and the RNA-binding protein HuR promotes it. HuR binds to a cis-element, HuRBS, located in the 3'UTR of the HMGB1 transcript, and at the same time miR-1192 is recruited to an adjacent seed element. The binding of HuR to the HuRBS prevents the recruitment of Argonaute 2 (Ago2), overriding miR-1192-mediated translation inhibition. Depleting HuR reduces myoblast fusion and silencing miR-1192 re-establishes the fusion potential of HuR-depleted cells. We propose that HuR promotes the commitment of myoblasts to myogenesis by enhancing the translation of HMGB1 and suppressing the translation inhibition mediated by miR-1192. RNA content was extracted following immunoprecipitation of HuR using a monoclonal antibody (3A2) and the levels of mRNA were compared to an IgG control in order to determine which transcripts were enriched in the HuR ribonucleoprotein complex.
2013-08-14 | E-GEOD-49855 | biostudies-arrayexpress
Project description:Upon muscle injury the high mobility group box 1 (HMGB1) protein is up-regulated and secreted to initiate reparative responses. Here we show that HMGB1 controls myogenesis both in vitro and in vivo, during development and after adult muscle injury. HMGB1 expression in muscle cells is regulated at the translational level: the miRNA miR-1192 inhibits HMGB1 translation and the RNA-binding protein HuR promotes it. HuR binds to a cis-element, HuRBS, located in the 3'UTR of the HMGB1 transcript, and at the same time miR-1192 is recruited to an adjacent seed element. The binding of HuR to the HuRBS prevents the recruitment of Argonaute 2 (Ago2), overriding miR-1192-mediated translation inhibition. Depleting HuR reduces myoblast fusion and silencing miR-1192 re-establishes the fusion potential of HuR-depleted cells. We propose that HuR promotes the commitment of myoblasts to myogenesis by enhancing the translation of HMGB1 and suppressing the translation inhibition mediated by miR-1192. RNA content was extracted following immunoprecipitation of HuR using a monoclonal antibody (3A2) and the levels of mRNA were compared to an IgG control in order to determine which transcripts were enriched in the HuR ribonucleoprotein complex.
2013-08-14 | E-GEOD-49856 | biostudies-arrayexpress
Project description:Upon muscle injury the high mobility group box 1 (HMGB1) protein is up-regulated and secreted to initiate reparative responses. Here we show that HMGB1 controls myogenesis both in vitro and in vivo, during development and after adult muscle injury. HMGB1 expression in muscle cells is regulated at the translational level: the miRNA miR-1192 inhibits HMGB1 translation and the RNA-binding protein HuR promotes it. HuR binds to a cis-element, HuRBS, located in the 3'UTR of the HMGB1 transcript, and at the same time miR-1192 is recruited to an adjacent seed element. The binding of HuR to the HuRBS prevents the recruitment of Argonaute 2 (Ago2), overriding miR-1192-mediated translation inhibition. Depleting HuR reduces myoblast fusion and silencing miR-1192 re-establishes the fusion potential of HuR-depleted cells. We propose that HuR promotes the commitment of myoblasts to myogenesis by enhancing the translation of HMGB1 and suppressing the translation inhibition mediated by miR-1192.
2013-08-14 | GSE49855 | GEO
Project description:Myoblast fusion is fundamental for the development of multinucleated myofibers. Evolutionarily conserved proteins required for myoblast fusion include Rac1 and its activator Dock1. Here, we tested the functions of Elmo proteins, Dock1-interacting scaffolds, on myoblast fusion. When Elmo1-/- mice underwent muscle-specific Elmo2 genetic ablation, they exhibited severe myoblast fusion defects. A mutation in the Elmo2 gene that reduced signaling resulted in a decrease in myoblast fusion. Conversely, a mutation in Elmo2 promoting its open conformation increased myoblast fusion during development and in muscle regeneration. Finally, we showed that the dystrophic features of the Dysferlin-null mice, a model of limb-girdle muscular dystrophy type 2B, were reversed when expressing Elmo2 in an open conformation. These data provide direct evidence that the myoblast fusion process could be exploited for regenerative and therapeutic purposes.
2022-07-25 | GSE209546 | GEO
Project description:The purpose of this study is to investigate how GDF10 regulates early myoblast differentiation and fusion. We found that melatonin can enhance fibro-adipogenic progenitors (FAPs) paracrine signaling to support muscle regeneration. Through combining transcriptome analysis and single-cell transcriptome analysis, we identified GDF10 as a type of myogenic factor specifically secreted by FAPs, which plays a beneficial role in promoting muscle fiber development and regeneration. To determine the underlying mechanism by which GDF10 regulates myogenesis, we performed RNA-seq on myoblasts treated with GDF10 or vehicle for 6 hours in vitro. We found that GDF10 promoted myoblast fusion by regulating LKB1-AMPK-MYOG-MYMK signaling during differentiation. In summary, our study revealed novel insights into the mechanism by which melatonin promotes muscle regeneration by mediating the interplay between FAPs and muscle stem cells (MuSCs).
2023-06-30 | GSE214164 | GEO
Project description:Upon muscle injury the high mobility group box 1 (HMGB1) protein is up-regulated and secreted to initiate reparative responses. Here we show that HMGB1 controls myogenesis both in vitro and in vivo, during development and after adult muscle injury. HMGB1 expression in muscle cells is regulated at the translational level: the miRNA miR-1192 inhibits HMGB1 translation and the RNA-binding protein HuR promotes it. HuR binds to a cis-element, HuRBS, located in the 3'UTR of the HMGB1 transcript, and at the same time miR-1192 is recruited to an adjacent seed element. The binding of HuR to the HuRBS prevents the recruitment of Argonaute 2 (Ago2), overriding miR-1192-mediated translation inhibition. Depleting HuR reduces myoblast fusion and silencing miR-1192 re-establishes the fusion potential of HuR-depleted cells. We propose that HuR promotes the commitment of myoblasts to myogenesis by enhancing the translation of HMGB1 and suppressing the translation inhibition mediated by miR-1192.
2013-08-14 | GSE49856 | GEO
Project description:Rbfox2-coordinated alternative splicing of Mef2d and Rock2 controls myoblast fusion during myogenesis
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