ArticleThe Biochemical journal1998
Mitsugumin29, a novel synaptophysin family member from the triad junction in skeletal muscle.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
45 citing papers in PubMed, 99 citations in OpenAlex.
- Reduced Synaptophysin-like 2 (MG29/SYPL2) Levels Mimic Age-Related Alterations in Skeletal Muscle Calcium Homeostasis and Lipid Signaling.Biomolecules · 2026Article
- Gait analysis for functional evaluation in a surgical hindlimb suspension model of muscle atrophy.The Journal of physiology · 2026Article
- Review
- 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
- Endoplasmic Reticulum-Plasma Membrane Junctions as Sites of Depolarization-Induced CaAnnual review of physiology · 2023Review
- The Sarcoplasmic Reticulum of Skeletal Muscle Cells: A Labyrinth of Membrane Contact Sites.Biomolecules · 2022Review
- Loss of dysferlin or myoferlin results in differential defects in excitation-contraction coupling in mouse skeletal muscle.Scientific reports · 2021Article
- Improper Remodeling of Organelles Deputed to CaInternational journal of molecular sciences · 2021Review
- Junctophilins: Key Membrane Tethers in Muscles and Neurons.Frontiers in molecular neuroscience · 2021Review
- Skeletal muscle: A review of molecular structure and function, in health and disease.Wiley interdisciplinary reviews. Systems biology and medicine · 2020Review
- Gene expression profiling of the early pathogenesis of wooden breast disease in commercial broiler chickens using RNA-sequencing.PloS one · 2018Article
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
- A focus on extracellular CaExperimental & molecular medicine · 2017Review
- Mitsugumin 29 regulates t-tubule architecture in the failing heart.Scientific reports · 2017Article
- Mitsugumin 53 regulates extracellular CaScientific reports · 2016Article
- Dual function of MG53 in membrane repair and insulin signaling.BMB reports · 2016Review
- Ca²⁺ microdomains organized by junctophilins.Cell calcium · 2015Review
- Interaction between mitsugumin 29 and TRPC3 participates in regulating Ca(2+) transients in skeletal muscle.Biochemical and biophysical research communications · 2015Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In skeletal muscle, excitation-contraction (E-C) coupling requires the conversion of the depolarization signal of the invaginated surface membrane, namely the transverse (T-) tubule, to Ca2+ release from the sarcoplasmic reticulum (SR). Signal transduction occurs at the junctional complex between the T-tubule and SR, designated as the triad junction, which contains two components essential for E-C coupling, namely the dihydropyridine receptor as the T-tubular voltage sensor and the ryanodine receptor as the SR Ca2+-release channel. However, functional expression of the two receptors seemed to constitute neither the signal-transduction system nor the junction between the surface and intracellular membranes in cultured cells, suggesting that some as-yet-unidentified molecules participate in both the machinery. In addition, the molecular basis of the formation of the triad junction is totally unknown. It is therefore important to examine the components localized to the triad junction. Here we report the identification using monoclonal antibody and primary structure by cDNA cloning of mitsugumin29, a novel transmembrane protein from the triad junction in skeletal muscle. This protein is homologous in amino acid sequence and shares characteristic structural features with the members of the synaptophysin family. The subcellular distribution and protein structure suggest that mitsugumin29 is involved in communication between the T-tubular and junctional SR membranes.
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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.