Group:MUZIC:Myopodin: Difference between revisions

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==Introduction== | ==Introduction== | ||
The protein myopodin (encoded by the gene SYNPO2[http://www.uniprot.org/uniprot/Q9UMS6]), also called synaptopodin-2, genethonin-2, synaptopodin-like and fesselin, is together with synaptopodin and tritopodin/CHAP a member of the podin protein family. It is widely expressed in striated, heart and smooth muscle cells where it localizes to Z-disks and dense bodies, respectively <ref name="r1"> PMID:11673475 </ref>. Myopodin is a multiadapter protein that interacts with filamentous actin, α-actinin and filamin. Different isoforms result from alternative splicing and alternative promoter usage and the predicted size of the resulting proteins varies between 74 kDa and 136 kDa; these variants show differential tissue distribution. The discrepancy between calculated molecular mass and apparent mobility in SDS-PAGE is at present still unclear, but might be due to post-translational modifications <ref> PMID:20554076 </ref> <ref> PMID:18371299 </ref> <ref> PMID:11696420</ref> <ref> PMID:12917631 </ref> <ref> PMID:18588515 </ref>. The lower molecular mass myopodin isoforms are dual compartment proteins that redistribute between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced manner <ref> PMID:C2150840 </ref>. Although its biological function is still undefined, recent findings support a role for myopodin as a z-disc multiadaptor protein (96). | The protein myopodin (encoded by the gene SYNPO2[http://www.uniprot.org/uniprot/Q9UMS6]), also called synaptopodin-2, genethonin-2, synaptopodin-like and fesselin, is together with synaptopodin and tritopodin/CHAP a member of the podin protein family. It is widely expressed in striated, heart and smooth muscle cells where it localizes to Z-disks and dense bodies, respectively <ref name="r1"> PMID:11673475 </ref>. Myopodin is a multiadapter protein that interacts with filamentous actin, α-actinin and filamin. Different isoforms result from alternative splicing and alternative promoter usage and the predicted size of the resulting proteins varies between 74 kDa and 136 kDa; these variants show differential tissue distribution. The discrepancy between calculated molecular mass and apparent mobility in SDS-PAGE is at present still unclear, but might be due to post-translational modifications <ref> PMID:20554076 </ref> <ref> PMID:18371299 </ref> <ref> PMID:11696420</ref> <ref> PMID:12917631 </ref> <ref> PMID:18588515 </ref>. The lower molecular mass myopodin isoforms are dual compartment proteins that redistribute between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced manner <ref> PMID:C2150840 </ref>. Although its biological function is still undefined, recent findings support a role for myopodin as a z-disc multiadaptor protein (96). |