Key result
JPH2 regulates mitochondrial function, metabolism, nuclear signaling, and immunity beyond classic structural coupling roles.
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Junctophilin-2 is a multifunctional protein with critical nonstructural roles in cardiomyocytes, including stress response and metabolism, extending beyond its known structural function in excitation-contraction coupling.
Junctophilin-2 (JPH2) is an essential structural protein that maintains the integrity of junctional membrane complexes (JMCs) in cardiomyocytes, thereby playing its canonical role in excitation-contraction (E-C) coupling. Recent studies reveal novel, nonstructural functions of JPH2 in cardiomyocytes, including regulation of mitochondrial function, lipid metabolism, nuclear signaling, and innate immune responses. Calpain-mediated cleavage of JPH2 generates nuclear fragments, which differentially modulate stress responses. Moreover, full-length JPH2 also localizes to the nucleus, where it forms phase-separated nuclear droplets during oxidative stress. Collectively, these findings highlight JPH2 as a multifunctional protein with critical roles beyond its canonical structural function in E-C coupling.
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Hutchison et al. (2025) reported a review. Junctophilin-2 (JPH2) was evaluated. Junctophilin-2 (JPH2) functions beyond its canonical structural role in excitation-contraction coupling to regulate mitochondrial function, lipid metabolism, nuclear signaling, and immune responses.
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