ArticleBiochemistry2010
Caveolin 3 is associated with the calcium release complex and is modified via in vivo triadin modification.
Article in Biochemistry, 2010. 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, 18 citations in OpenAlex.
- Electrical Conduction System Remodeling in Streptozotocin-Induced Diabetes Mellitus Rat Heart.Frontiers in physiology · 2019Article
- Three residues in the luminal domain of triadin impact on Trisk 95 activation of skeletal muscle ryanodine receptors.Pflugers Archiv : European journal of physiology · 2016Article
- Caveolae as plasma membrane sensors, protectors and organizers.Nature reviews. Molecular cell biology · 2013Review
- A family with discordance between malignant hyperthermia susceptibility and rippling muscle disease.Journal of anesthesia · 2013Article
- Palmitate diet-induced loss of cardiac caveolin-3: a novel mechanism for lipid-induced contractile dysfunction.PloS one · 2013Article
- Characterization of the molecular architecture of human caveolin-3 and interaction with the skeletal muscle ryanodine receptor.The Journal of biological chemistry · 2012Article
- Junctophilin 1 and 2 proteins interact with the L-type Ca2+ channel dihydropyridine receptors (DHPRs) in skeletal muscle.The Journal of biological chemistry · 2011Article
- Alterations of excitation-contraction coupling and excitation coupled Ca(2+) entry in human myotubes carrying CAV3 mutations linked to rippling muscle.Human mutation · 2011Article
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
Abstract
The triadin isoforms Trisk 95 and Trisk 51 are both components of the skeletal muscle calcium release complex. To investigate the specific role of Trisk 95 and Trisk 51 isoforms in muscle physiology, we overexpressed Trisk 95 or Trisk 51 using adenovirus-mediated gene transfer in skeletal muscle of newborn mice. Overexpression of either Trisk 95 or Trisk 51 alters the muscle fiber morphology, while leaving unchanged the expression of the ryanodine receptor, the dihydropyridine receptor, and calsequestrin. We also observe an aberrant expression of caveolin 3 in both Trisk 95- and Trisk 51-overexpressing skeletal muscles. Using a biochemical approach, we demonstrate that caveolin 3 is associated with the calcium release complex in skeletal muscle. Taking advantage of muscle and non-muscle cell culture models and triadin null mouse skeletal muscle, we further dissect the molecular organization of the caveolin 3-containing calcium release complex. Our data demonstrate that the association of caveolin 3 with the calcium release complex occurs via a direct interaction with the transmembrane domain of the ryanodine receptor. Taken together, these data suggest that caveolin 3-containing membrane domains and the calcium release complex are functionally linked and that Trisk 95 and Trisk 51 are instrumental to the regulation of this interaction, the integrity of which may be crucial for muscle physiology.
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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.