ArticleExperimental & molecular medicine2016
Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle.
Article in Experimental & molecular medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 18 citations in OpenAlex.
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- Sumoylation-deficient phosphoglycerate mutase 2 impairs myogenic differentiation.Frontiers in cell and developmental biology · 2022Article
- An Adult Mouse Model of Dilated Cardiomyopathy Caused by Inducible Cardiac-SpecificInternational journal of molecular sciences · 2021Article
- Chaperone-Assisted Mitotic Actin Remodeling by BAG3 and HSPB8 Involves the Deacetylase HDAC6 and Its Substrate Cortactin.International journal of molecular sciences · 2020Article
- Under construction: The dynamic assembly, maintenance, and degradation of the cardiac sarcomere.Journal of molecular and cellular cardiology · 2020Review
- Multi-Cellular Functions of MG53 in Muscle Calcium Signaling and Regeneration.Frontiers in physiology · 2020Review
- An MG53-IRS1-interaction disruptor ameliorates insulin resistance.Experimental & molecular medicine · 2018Article
- Fine-tuning of actin dynamics by the HSPB8-BAG3 chaperone complex facilitates cytokinesis and contributes to its impact on cell division.Cell stress & chaperones · 2017Article
- Mesenchymal stem cells and myoblast differentiation under HGF and IGF-1 stimulation for 3D skeletal muscle tissue engineering.BMC cell biology · 2017Article
- Heat Shock Factor 1 Depletion Sensitizes A172 Glioblastoma Cells to Temozolomide via Suppression of Cancer Stem Cell-Like Properties.International journal of molecular sciences · 2017Article
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8 authors at 3 institutions in 1 country.
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Abstract
BCL-2 interacting cell death suppressor (BIS), which is ubiquitously expressed, has important roles in various cellular processes, such as apoptosis, the cellular stress response, migration and invasion and protein quality control. In particular, BIS is highly expressed in skeletal and cardiac muscles, and BIS gene mutations result in human myopathy. In this study, we show that mRNA and protein levels of BIS were markedly increased during skeletal myogenesis in C2C12 cells and mouse satellite cells. BIS knockdown did not prevent the early stage of skeletal myogenesis, but did induce muscle atrophy and a decrease in the diameter of myotubes. BIS knockdown significantly suppressed the expression level of myosin heavy chain (MyHC) without changing the expression levels of myogenic marker proteins, such as Mgn, Cav-3 and MG53. In addition, BIS endogenously interacted with MyHC, and BIS knockdown induced MyHC ubiquitination and degradation. From these data, we conclude that molecular association of MyHC and BIS is necessary for MyHC stabilization in skeletal muscle.
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