Key result
Phosphorylation of myopodin by PKA or CaMKII mediates 14-3-3 binding and nuclear import, while dephosphorylation by calcineurin abrogates this binding, regulating myopodin trafficking in cardiac myocytes.
The identification of myopodin as a direct target of PKA, CaMKII, and calcineurin defines a novel intracellular signaling pathway whereby changes in Z-disc dynamics may translate into compartmentalized signal transduction in the heart.
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May inform compartmentalized signaling studies in heart failure; leaves open therapeutic targeting of myopodin trafficking pending human validation.
Faul et al. (2007) studied Cardiac myocyte signaling. PKA, CaMKII, and calcineurin modulation was evaluated on Subcellular localization and phosphorylation of myopodin. Phosphorylation of myopodin by PKA or CaMKII mediates 14-3-3 binding and nuclear import, while dephosphorylation by calcineurin abrogates this binding, regulating myopodin trafficking in cardiac myocytes.
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