Group:MUZIC:Myopodin - Revision history

Jaime Prilusky at 11:32, 1 July 2015

Jaime Prilusky — Wed, 01 Jul 2015 11:32:28 GMT

←Older revision		Revision as of 11:32, 1 July 2015
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	==References==		==References==
	<references/>		<references/>
		+	[[Category: Z-disk]]

Nikos Pinotsis at 11:41, 2 April 2013

Nikos Pinotsis — Tue, 02 Apr 2013 11:41:53 GMT

←Older revision		Revision as of 11:41, 2 April 2013
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	==Sequence Annotation==		==Sequence Annotation==
-	Myopodin contains one PPXY motif and multiple PXXP motifs <ref name="r1"> 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>.	+	Myopodin contains one PPXY motif and multiple PXXP motifs <ref name="r1"> 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 Ca<sup>2+</sup>/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>.


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	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>.		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>.
	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>.		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, ~~Casup~~>2+</sup>/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, Ca<sup>2+</sup>/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 Filamin C.jpg\|700px]]		[[Image:Myopodin interaction with Filamin C.jpg\|700px]]

Nikos Pinotsis at 11:41, 2 April 2013

Nikos Pinotsis — Tue, 02 Apr 2013 11:41:06 GMT

←Older revision		Revision as of 11:41, 2 April 2013
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	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>.		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>.
	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>.		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, Casup>2+</sup>/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 Filamin C.jpg\|700px]]		[[Image:Myopodin interaction with Filamin C.jpg\|700px]]

Nikos Pinotsis at 11:39, 2 April 2013

Nikos Pinotsis — Tue, 02 Apr 2013 11:39:12 GMT

←Older revision		Revision as of 11:39, 2 April 2013
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	==Introduction==		==Introduction==
-	The protein synaptopodin-2 (encoded by the gene SYNPO2[http://www.uniprot.org/uniprot/Q9UMS6]), also called "myopodin", 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 synaptopodin-2 (encoded by the gene SYNPO2[http://www.uniprot.org/uniprot/Q9UMS6]), also called '''myopodin''', 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).

	==Sequence Annotation==		==Sequence Annotation==

Nikos Pinotsis at 11:36, 2 April 2013

Nikos Pinotsis — Tue, 02 Apr 2013 11:36:16 GMT

←Older revision		Revision as of 11:36, 2 April 2013
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		+	===Synaptopodin-2===
		+
	==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 synaptopodin-2 (encoded by the gene SYNPO2[http://www.uniprot.org/uniprot/Q9UMS6]), also called "myopodin", 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).

	==Sequence Annotation==		==Sequence Annotation==

Nikos Pinotsis at 11:33, 2 April 2013

Nikos Pinotsis — Tue, 02 Apr 2013 11:33:13 GMT

←Older revision		Revision as of 11:33, 2 April 2013
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-	<Structure load='MYO_PDZ_BD.pdb' size='400' frame='true' align='right' caption='Prediction of the PDZ binding domain of Myopodin . Lambert et al. ESyPred3D:Prediction of Proteins 3D structures. Bioinformatics 2002)' scene='Insert optional scene name here' />
-
	==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).

Nikos Pinotsis at 13:28, 5 March 2013

Nikos Pinotsis — Tue, 05 Mar 2013 13:28:36 GMT

←Older revision		Revision as of 13:28, 5 March 2013
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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> 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).

	==Sequence Annotation==		==Sequence Annotation==
-	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>.	+	Myopodin contains one PPXY motif and multiple PXXP motifs <ref name="r1"> 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>.


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	==Function==		==Function==
-	Myopodin is a dual compartment protein that redistributes between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced fashion, and in addition displays actin-bundling activity <ref> PMID:11673475 </ref>.	+	Myopodin is a dual compartment protein that redistributes between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced fashion, and in addition displays actin-bundling activity <ref name="r1"> PMID:11673475 </ref>.
-	In undifferentiated myoblasts, myopodin seems to be expressed preferentially in the nucleus and only weakly in the cytoplasm, whereas in differentiating myotubes, myopodin is incorporated into the Z-disc with no detectable nuclear expression, suggesting that myopodin may be involved in the regulation of myocyte differentiation <ref> PMID:11673475 </ref> <ref> PMID:19360353 </ref>.	+	In undifferentiated myoblasts, myopodin seems to be expressed preferentially in the nucleus and only weakly in the cytoplasm, whereas in differentiating myotubes, myopodin is incorporated into the Z-disc with no detectable nuclear expression, suggesting that myopodin may be involved in the regulation of myocyte differentiation <ref name="r1"> PMID:11673475 </ref> <ref> PMID:19360353 </ref>.
	Myopodin has also been identified as a tumor suppressor gene that is frequently deleted in aggressive prostate cancer <ref> PMID:15111326 </ref>. Expression of myopodin protein suppresses both tumor growth and metastasis in vitro and in vivo <ref> PMID:15111326 </ref>.		Myopodin has also been identified as a tumor suppressor gene that is frequently deleted in aggressive prostate cancer <ref> PMID:15111326 </ref>. Expression of myopodin protein suppresses both tumor growth and metastasis in vitro and in vivo <ref> PMID:15111326 </ref>.

	== Myopodin Interactions ==		== 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 <ref> PMID:11673475 </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 name="r1"> PMID:11673475 </ref>.
	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>.		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>.		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>.

Irela Gretchen Reza Mazar at 11:24, 11 January 2013

Irela Gretchen Reza Mazar — Fri, 11 Jan 2013 11:24:24 GMT

←Older revision		Revision as of 11:24, 11 January 2013
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	==Pathology==		==Pathology==
-	The SYNPO2 gene frequently exhibits deletions in aggresive prostate cancer tissues <ref> PMID:11696420</ref>. Myopodin was suggested to play a role as tumor suppressor, because in normal urothelium of the bladder myopodin is localized both in the cytoplasm and in the nucleus, wheras in superficial and invasive bladder tumors, reduced nuclear expression of myopodin was observed <ref> PMID:12917631 </ref>. The expression of myopodin suppressed tumor growth and metastasis <ref> PMID:15111326 </ref>.	+	The SYNPO2 gene frequently exhibits deletions in aggresive prostate cancer tissues and statistical analysis indicates that deletion of myopodin is highly correlated with the invasiveness of prostate cancers, and thus may hold promise as an important prognostic marker for prostate cancers <ref> PMID:11696420</ref>. Myopodin was suggested to play a role as tumor suppressor, because in normal urothelium of the bladder myopodin is localized both in the cytoplasm and in the nucleus, wheras in superficial and invasive bladder tumors, reduced nuclear expression of myopodin was observed <ref> PMID:12917631 </ref>. The expression of myopodin suppressed tumor growth and metastasis <ref> PMID:15111326 </ref>.

	==References==		==References==
	<references/>		<references/>

Irela Gretchen Reza Mazar at 18:58, 10 January 2013

Irela Gretchen Reza Mazar — Thu, 10 Jan 2013 18:58:49 GMT

←Older revision		Revision as of 18:58, 10 January 2013
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	==Sequence Annotation==		==Sequence Annotation==
	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>.		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]]		[[Image:Myopodin.jpg\|800px]]

Irela Gretchen Reza Mazar at 18:58, 10 January 2013

Irela Gretchen Reza Mazar — Thu, 10 Jan 2013 18:58:22 GMT

←Older revision		Revision as of 18:58, 10 January 2013
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	==Sequence Annotation==		==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]]		[[Image:Myopodin.jpg\|800px]]