Group:MUZIC:Myopodin: Difference between revisions

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Myopodin also binds to α-actinin via its spectrin repeats <ref> PMID:16450054 </ref>, <ref> PMID:20554076 </ref> . Myopodin may be generally involved in the organization and anchoring of actin in muscle cells and might be required for the correct localization of α-actinin. This hypothesis is supported by recent findings where myopodin expression precedes actin and α-actinin expression <ref> PMID:20554076 </ref>.

A filamin-binding region was mapped to a fragment encompassing amino acids 240–521 of myopodin, i.e. a region that contains two of the previously described homology regions shared by myopodin and synaptopodin <ref> PMID:20554076 </ref>.

~~Through yeast~~ two-hybrid analysis, ~~was found the interaction between Myopodin and Zyxin both in vitro and in vivo and that this interaction~~ leads to slower migration of prostate cancer cells and reduced invasiveness <ref> PMID:16885336 </ref>.

Yeast two-hybrid analysis also identified an interaction of myopodin with zyxin, which leads to slower migration of prostate cancer cells and reduced invasiveness <ref> PMID:16885336 </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>.

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 FLNC.jpg|700px]]

@@ Line 18: / Line 18: @@
 Myopodin also binds to α-actinin via its spectrin repeats <ref> PMID:16450054 </ref>, <ref> PMID:20554076 </ref> . Myopodin may be generally involved in the organization and anchoring of actin in muscle cells and might be required for the correct localization of α-actinin. This hypothesis is supported by recent findings where myopodin expression precedes actin and α-actinin expression <ref> PMID:20554076 </ref>.
 A filamin-binding region was mapped to a fragment encompassing amino acids 240–521 of myopodin, i.e. a region that contains two of the previously described homology regions shared by myopodin and synaptopodin <ref> PMID:20554076 </ref>.
-Through yeast two-hybrid analysis, was found the interaction between Myopodin and Zyxin both in vitro and in vivo and that this interaction leads to slower migration of prostate cancer cells and reduced invasiveness <ref> PMID:16885336 </ref>.
+Yeast two-hybrid analysis also identified an interaction  of myopodin with zyxin, which leads to slower migration of prostate cancer cells and reduced invasiveness <ref> PMID:16885336 </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>.
+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 FLNC.jpg|700px]]