Journal
CHANNELS
Volume 5, Issue 5, Pages 389-394Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/chan.5.5.16467
Keywords
striated muscle; junctional membrane; immune-proteomic approach; calcium homeostasis; junctophilin; mitsugumin 29; trimeric intracellular cation channel
Categories
Funding
- Grants-in-Aid for Scientific Research [23136506, 22790209, 23659037] Funding Source: KAKEN
- NIA NIH HHS [R01 AG015556, R01 AG028856] Funding Source: Medline
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Ca2+ signaling in skeletal and cardiac muscles is a bi-directional process that involves cross-talk between signaling molecules in the sarcolemmal membrane and Ca2+ release machinery in the intracellular organelles. Maintenance of a junctional membrane structure between the sarcolemmal membrane and the sarcoplasmic reticulum (SR) provides a framework for the conversion of action potential arrived at the sarcolemma into release of Ca2+ from the SR, leading to activation of a variety of physiological processes. Activity-dependent changes in Ca2+ storage inside the SR provides a retrograde signal for the activation of store-operated Ca2+ channel (SOC) on the sarcolemmal membrane, which plays important roles in the maintenance of Ca2+ homeostasis in physiology and pathophysiology. Research progress during the last 30 years had advanced our understanding of the cellular and molecular mechanisms for the control of Ca2+ signaling in muscle and cardiovascular physiology. Here we summarize the functions of three key molecules that are located in the junctional membrane complex of skeletal and cardiac muscle cells: junctophilin as a glue that physiologically links the SR membrane to the sarcolemmal membrane for formation of the junctional membrane framework, mitsugumin29 as a muscle-specific synaptophysin family protein that contributes to maintain the coordinated Ca2+ signaling in skeletal muscle, and trimeric intracellular cation channel as a novel cation-selective channel located on the SR membrane that provides counter-ion current during the rapid process of Ca2+ release from the SR.
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