ArticleCell & bioscience2021
BVES is a novel interactor of ANO5 and regulates myoblast differentiation.
Article in Cell & bioscience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Diosbulbin B attenuates propylthiouracil-induced thyroid enlargement in mice by regulating the gut microbiota-short chain fatty acids-thyroid axis.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Anoctamin-5 deficiency enhances ATG9A-dependent autophagy, inducing osteogenesis and gnathodiaphyseal dysplasia-like bone formation.JCI insight · 2025Article
- In vitro enzymatic and cell culture assays for SARS-CoV-2 main protease interaction with ambenonium.Scientific reports · 2025Article
- TMEM16 proteins: CaInternational journal of molecular medicine · 2024Review
- Defective BVES-mediated feedback control of cAMP in muscular dystrophy.Nature communications · 2023Article
- Systemic AAV9.BVES delivery ameliorates muscular dystrophy in a mouse model of LGMDR25.Molecular therapy : the journal of the American Society of Gene Therapy · 2023Article
- Differential effects of mutations of POPDC proteins on heteromeric interaction and membrane trafficking.Acta neuropathologica communications · 2023Article
- The Role of POPDC Proteins in Cardiac Pacemaking and Conduction.Journal of cardiovascular development and disease · 2021Review
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundAnoctamin 5 (ANO5) is a membrane protein belonging to the TMEM16/Anoctamin family and its deficiency leads to the development of limb girdle muscular dystrophy R12 (LGMDR12). However, little has been known about the interactome of ANO5 and its cellular functions.
resultsIn this study, we exploited a proximal labeling approach to identify the interacting proteins of ANO5 in C2C12 myoblasts stably expressing ANO5 tagged with BioID2. Mass spectrometry identified 41 unique proteins including BVES and POPDC3 specifically from ANO5-BioID2 samples, but not from BioID2 fused with ANO6 or MG53. The interaction between ANO5 and BVES was further confirmed by co-immunoprecipitation (Co-IP), and the N-terminus of ANO5 mediated the interaction with the C-terminus of BVES. ANO5 and BVES were co-localized in muscle cells and enriched at the endoplasmic reticulum (ER) membrane. Genome editing-mediated ANO5 or BVES disruption significantly suppressed C2C12 myoblast differentiation with little impact on proliferation.
conclusionsTaken together, these data suggest that BVES is a novel interacting protein of ANO5, involved in regulation of muscle differentiation.
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