PFN1 Inhibits Myogenesis of Bovine Myoblast Cells via Cdc42-PAK/JNK

• Published in: Cells (Basel, Switzerland) Vol. 11; no. 20; p. 3188
• Main Authors: Zi, Jingjing, Xu, Jing, Luo, Jintang, Yang, Xu, Zhen, Zhen, Li, Xin, Hu, Debao, Guo, Yiwen, Guo, Hong, Ding, Xiangbin, Zhang, Linlin
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01.10.2022; MDPI
• Subjects: Actin; Actins; Amyotrophic lateral sclerosis; Animals; Antibodies; Binding proteins; bovine; c-Jun protein; Cattle; Cdc42; Cdc42 protein; Cell cycle; Cell Differentiation; Cell division; Cell growth; Cytoskeleton; Gene expression; Health aspects; Immunoprecipitation; JNK Mitogen-Activated Protein Kinases; JNK protein; Mass spectroscopy; Muscle cells; Muscle Development; Muscles; Musculoskeletal system; Mutation; Myoblasts; Myogenesis; myogenic differentiation; PAK; PFN1; Phosphorylation; Phosphotransferases; Plasmids; Prevention; Proteins; Satellite cells; Satellite Cells, Skeletal Muscle; Skeletal muscle; skeletal muscle satellite cells; Transcription factors; China; Beijing China; United Kingdom > UK; United States > US; JNK; myogenic differentiation; bovine; skeletal muscle satellite cells; PAK; PFN1; Cdc42
• ISSN: 2073-4409; 2073-4409
• DOI: 10.3390/cells11203188

Myoblast differentiation is essential for the formation of skeletal muscle myofibers. Profilin1 (Pfn1) has been identified as an actin-associated protein, and has been shown to be critically important to cellular function. Our previous study found that PFN1 may inhibit the differentiation of bovine skeletal muscle satellite cells, but the underlying mechanism is not known. Here, we confirmed that PFN1 negatively regulated the myogenic differentiation of bovine skeletal muscle satellite cells. Immunoprecipitation assay combined with mass spectrometry showed that Cdc42 was a binding protein of PFN1. Cdc42 could be activated by PFN1 and could inhibit the myogenic differentiation like PFN1. Mechanistically, activated Cdc42 increased the phosphorylation level of p2l-activated kinase (PAK), which further activated the phosphorylation activity of c-Jun N-terminal kinase (JNK), whereas PAK and JNK are inhibitors of myogenic differentiation. Taken together, our results reveal that PFN1 is a repressor of bovine myogenic differentiation, and provide the regulatory mechanism.