Group:MUZIC:Myopodin: Difference between revisions
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In cardiomyocytes, myopodin forms a Z-disc signaling complex with α-actinin, calcineurin, Ca2+/calmodulin-dependent kinase II (CaMKII), muscle-specific A-kinase anchoring protein, and myomegalin. Calcineurin keeps myopodin dephosphorylated preventing 14-3-3ß binding to myopodin. Upon activation of PKA/CaMKII or inhibition of calcineurin, myopodin undergoes phosphorylation, enabling its interaction with 14-3-3ß, which releases myopodin from the Z-disc-anchoring proteins and induces its nuclear import. This novel intracellular signaling pathway suggests that changes in Z-disc dynamics may translate into compartmentalized signal transduction in the heart <ref> PMID:17923693 </ref>. | In cardiomyocytes, myopodin forms a Z-disc signaling complex with α-actinin, calcineurin, Ca2+/calmodulin-dependent kinase II (CaMKII), muscle-specific A-kinase anchoring protein, and myomegalin. Calcineurin keeps myopodin dephosphorylated preventing 14-3-3ß binding to myopodin. Upon activation of PKA/CaMKII or inhibition of calcineurin, myopodin undergoes phosphorylation, enabling its interaction with 14-3-3ß, which releases myopodin from the Z-disc-anchoring proteins and induces its nuclear import. This novel intracellular signaling pathway suggests that changes in Z-disc dynamics may translate into compartmentalized signal transduction in the heart <ref> PMID:17923693 </ref>. | ||
[[Image:Myopodin interaction with | [[Image:Myopodin interaction with Filamin C.jpg|700px]] | ||
[[Image:Model for the regulation of Myopodin's subcellular localization in Cardiomyocytes.jpg|700px]] | [[Image:Model for the regulation of Myopodin's subcellular localization in Cardiomyocytes.jpg|700px]] | ||