Group:MUZIC:Myopodin: Difference between revisions

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== Myopodin Interactions ==

Actin was the first binding partner of myopodin to be identified. Actin binding was narrowed down to residues 410–563 of murine myopodin. site <ref> PMID:11673475 </ref> that was identified by producing truncated fragments from myopodin and the smallest fragment that bound to F-actin contained residues 410–563 of mouse Myopodin. Actin has an essential role in anchoring Myopodin into the Z-disc <ref> PMID:11673475 ~~</ref> <ref> PMID:17923693~~ </ref>.

Actin was the first binding partner of myopodin to be identified. Actin binding was narrowed down to residues 410–563 of murine myopodin <ref> PMID:11673475 </ref>.

Myopodin binds to α-actinin ~~and this interaction has been shown to involve the Spectrin filament domain repeat region of α-actinin~~ <ref> PMID:16450054 </ref>. It's believed that synaptopodin family members are involved in the organization and anchoring of actin in the cell and might be necessary 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>.

Myopodin also binds to α-actinin via its spectrin repeats <ref> PMID:16450054 </ref>. It's believed that synaptopodin family members are involved in the organization and anchoring of actin in the cell and might be necessary 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 newly identiﬁed filamin-binding region within the molecule was reported by performing yeast two-hybrid assays using carboxy-terminally and/or amino-terminally truncated constructs <ref> PMID:20554076 </ref>. The interaction 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:11696420 </ref>. The alternative transcription offers the possibility of expression of two isoforms of Myopodin, which probably differ in their binding properties for these PDZ binding domain detected, however, there is preliminary evidence that the PDZ binding domain from Myopodin interacts with the C terminal part of Synemin <ref> PMID:16631741 </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>.

@@ Line 15: / Line 15: @@
 == Myopodin Interactions ==
-Actin was the first binding partner of myopodin to be identified. Actin binding was narrowed down to residues 410–563 of murine myopodin. site <ref> PMID:11673475 </ref> that was identified by producing truncated fragments from myopodin and the smallest fragment that bound to F-actin contained residues 410–563 of mouse Myopodin. Actin has an essential role in anchoring Myopodin into the Z-disc <ref> PMID:11673475 </ref> <ref> PMID:17923693 </ref>.
+Actin was the first binding partner of myopodin to be identified. Actin binding was narrowed down to residues 410–563 of murine myopodin <ref> PMID:11673475 </ref>.
-Myopodin binds to α-actinin and this interaction has been shown to involve the Spectrin  filament domain repeat region of α-actinin <ref> PMID:16450054 </ref>. It's believed that synaptopodin family members are involved in the organization and anchoring of actin in the cell and might be necessary 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>.
+Myopodin also binds to α-actinin via its spectrin repeats <ref> PMID:16450054 </ref>. It's believed that synaptopodin family members are involved in the organization and anchoring of actin in the cell and might be necessary 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 newly identiﬁed filamin-binding region within the molecule was reported by performing yeast two-hybrid assays using carboxy-terminally and/or amino-terminally truncated constructs <ref> PMID:20554076 </ref>. The interaction 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:11696420 </ref>. The alternative transcription offers the possibility of expression of two isoforms of Myopodin, which probably differ in their binding properties for these PDZ binding domain detected, however, there is preliminary evidence that the PDZ binding domain from Myopodin interacts with the C terminal part of Synemin <ref> PMID:16631741 </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>.