ArticleBiochemical and biophysical research communications2015
Interaction between mitsugumin 29 and TRPC3 participates in regulating Ca(2+) transients in skeletal muscle.
Article in Biochemical and biophysical research communications, 2015. 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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Who cites it
12 citing papers in PubMed, 14 citations in OpenAlex.
- Architecture and molecular machinery of skeletal myofibers: a systematic review of the structure-function relationships.Frontiers in cell and developmental biology · 2025Review
- Branched-chain amino acids and L-alanine supplementation ameliorate calcium dyshomeostasis in sarcopenia: New insights for nutritional interventions.Frontiers in pharmacology · 2024Article
- Sarcoplasmic Reticulum CaCells · 2023Review
- The Sarcoplasmic Reticulum of Skeletal Muscle Cells: A Labyrinth of Membrane Contact Sites.Biomolecules · 2022Review
- Structure-function relationships and modifications of cardiac sarcoplasmic reticulum Ca2+-transport.Physiological research · 2021Review
- Distinct glycolytic pathway regulation in liver, tumour and skeletal muscle of mice with cancer cachexia.Cell biochemistry and function · 2021Article
- TRPC channels in exercise-mimetic therapy.Pflugers Archiv : European journal of physiology · 2019Review
- STIM2 regulates both intracellular CaScientific reports · 2017Article
- A focus on extracellular CaExperimental & molecular medicine · 2017Review
- Mitsugumin 29 regulates t-tubule architecture in the failing heart.Scientific reports · 2017Article
- Review
- Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers.Journal of muscle research and cell motility · 2015Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Mitsugumin 29 (MG29) is related to the fatigue and aging processes of skeletal muscle. To examine the roles of MG29 in conjunction with its binding protein, the canonical-type transient receptor potential cation channel 3 (TRPC3), in skeletal muscle, the binding region of MG29 to TRPC3 was studied along with the functional relevance of the binding in mouse primary skeletal myotubes using co-immunoprecipitation assays and Ca(2+) imaging experiments. The N-terminus and the I-II loop of MG29 constitute the binding region for TRPC3. The myotubes that expressed the MG29 mutant missing the entire TRPC3-binding region showed a disrupted binding between endogenous MG29 and TRPC3 and a reduction in Ca(2+) transients in response to membrane depolarization without affecting ryanodine receptor 1 activity, the resting cytosolic Ca(2+) level, and the amount of releasable Ca(2+) from the sarcoplasmic reticulum. Among the proteins mediating Ca(2+) movements in skeletal muscle, TRPC4 expression was significantly decreased by the MG29 mutant. Therefore, MG29 could be a new factor for regulating Ca(2+) transients during skeletal muscle contraction possibly via a correlation with TRPC3 and TRPC4.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.