Group:MUZIC:Myopodin: Difference between revisions

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==Sequence Annotation==

Myopodin contains one PPXY motif and multiple PXXP motifs. Beside 2 lysine-rich NLS sites (consensus motif K-K/RX-K/R) myopodin provides 2 binding sites for 14-3-3(consensus motif a: RSXpS/TXP; b: RXXXpS/TXP Biophys Rev (2010) 2:181-189). These sites seem to be indispensable for effective shuttling of myopodin from the Z-disk into the nucleus <ref> PMCID:PMC2171942 </ref>. Phosphorylation of myopodin within the 14-3-3 binding sites (S225 and T272) by protein kinase A and Ca2+/calmodulin-dependent protein kinase II abrogates the binding with α -actinin and promotes the binding with 14-3-3 and importin α <ref> PMID:17923693 </ref>. Another important domain present in myopodin is the PDZ domain (postsynaptic density 95, discs large, and zonula occludens-1). PDZ domains are protein-protein interaction modules that can mediate multiple biological processes such as vesicle transport, ion channel signaling, and signal transduction in several tissues. PDZ domains in myopodin are of unknown function <ref> PMID:18371299 </ref>.

Myopodin contains one PPXY motif and multiple PXXP motifs <ref> PMID:11673475 </ref>. Beside 2 lysine-rich NLS sites (consensus motif K-K/RX-K/R) myopodin provides 2 binding sites for 14-3-3(consensus motif a: RSXpS/TXP; b: RXXXpS/TXP Biophys Rev (2010) 2:181-189). These sites seem to be indispensable for effective shuttling of myopodin from the Z-disk into the nucleus <ref> PMCID:PMC2171942 </ref>. Phosphorylation of myopodin within the 14-3-3 binding sites (S225 and T272) by protein kinase A and Ca2+/calmodulin-dependent protein kinase II abrogates the binding with α -actinin and promotes the binding with 14-3-3 and importin α <ref> PMID:17923693 </ref>. Another important domain present in myopodin is the PDZ domain (postsynaptic density 95, discs large, and zonula occludens-1). PDZ domains are protein-protein interaction modules that can mediate multiple biological processes such as vesicle transport, ion channel signaling, and signal transduction in several tissues. PDZ domains in myopodin are of unknown function <ref> PMID:18371299 </ref>.

[[Image:Myopodin.jpg|800px]]

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 ==Sequence Annotation==
-Myopodin contains one PPXY motif and multiple PXXP motifs. Beside 2 lysine-rich NLS sites (consensus motif K-K/RX-K/R) myopodin provides 2 binding sites for 14-3-3(consensus motif a: RSXpS/TXP; b: RXXXpS/TXP Biophys Rev (2010) 2:181-189). These sites seem to be indispensable for effective shuttling of myopodin from the Z-disk into the nucleus <ref> PMCID:PMC2171942 </ref>. Phosphorylation of myopodin within the 14-3-3 binding sites (S225 and T272) by protein kinase A and Ca2+/calmodulin-dependent protein kinase II abrogates the binding with α -actinin and promotes the binding with 14-3-3 and importin α <ref> PMID:17923693 </ref>. Another important domain present in myopodin is the PDZ domain (postsynaptic density 95, discs large, and zonula occludens-1). PDZ domains are protein-protein interaction modules that can mediate multiple biological processes such as vesicle transport, ion channel signaling, and signal transduction in several tissues. PDZ domains in myopodin are of unknown function <ref> PMID:18371299 </ref>.
+Myopodin contains one PPXY motif and multiple PXXP motifs <ref> PMID:11673475 </ref>. Beside 2 lysine-rich NLS sites (consensus motif K-K/RX-K/R) myopodin provides 2 binding sites for 14-3-3(consensus motif a: RSXpS/TXP; b: RXXXpS/TXP Biophys Rev (2010) 2:181-189). These sites seem to be indispensable for effective shuttling of myopodin from the Z-disk into the nucleus <ref> PMCID:PMC2171942 </ref>. Phosphorylation of myopodin within the 14-3-3 binding sites (S225 and T272) by protein kinase A and Ca2+/calmodulin-dependent protein kinase II abrogates the binding with α -actinin and promotes the binding with 14-3-3 and importin α <ref> PMID:17923693 </ref>. Another important domain present in myopodin is the PDZ domain (postsynaptic density 95, discs large, and zonula occludens-1). PDZ domains are protein-protein interaction modules that can mediate multiple biological processes such as vesicle transport, ion channel signaling, and signal transduction in several tissues. PDZ domains in myopodin are of unknown function <ref> PMID:18371299 </ref>.
 [[Image:Myopodin.jpg|800px]]