Proteopedia - User contributions [en]

Group:MUZIC:Synaptopodin

2013-02-08T17:52:52Z

Eduardo Bezerra: /* Pathology */

== Introduction ==

Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes and in muscle cells is exclusively expressed in terminally differentiated skeletal muscle cells, where is colocalized with alpha-actinin and filamin C in the Z-disc. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.

== Sequence annotation ==

The protein KIBRA localized in podocytes directly bind to synaptopodin via the WW domains. The long variant of synaptopodin (903 aa) that is expressed in podocytes contains two internal PPxY sites, two PEST sequences, an actin-binding domain, and four α-actinin–binding regions (Duning et al. 2008)<ref>PMID: 18596123</ref>.

[[Image:Synaptopodin_isoforms.png|700px|left|thumb|Synaptopodin exist in three different isoforms produced by alternative splicing of the N- and C-terminal exons.]]

== Structure ==
There is no structure related for this protein.

== Function and interactions ==

The high degree of sequence similarity between the three members of the podin family in defined regions suggests analog binding properties. Indeed, biochemical studies revealed that all podin proteins interact with the Ig-domains 20-21 of filamin C. Similar to the situation in synaptopodin interaction studies showed that alpha-actinin binds also myopodin and tritopodin at multiple binding sites.(Linnemann et al. 2010)<ref>PMID:20554076</ref>.Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

Members of the podin family have been implicated in cancers. Synaptopodin 2 (myopodin) is expressed primarily in nuclei of proliferating myoblast cells. Cytoplasmic Synaptopodin 2 appears within hours of differentiation of myoblasts into myotubes and is found in Z-lines of mature myotubes. Like myopodin, synaptopodin associates with actin and appears to display actin-bundling activity, where is frequently absent in invasive prostate cancer and may serve as a prognostic marker for prostate cancers. (Weins et al. 2001)<ref>PMID:11673475 </ref>.
There is another level of complexity regarding the role of actin bundling proteins in cancer. Metastasis requires cell motility, a property normally associated with plasticity of actin filaments. However, there is ample evidence that bundling of actin filaments is a prerequisite for formation of invadosomes. Elevated levels of some actin bundling proteins are associated with more aggressive cancer phenotypes.(Iguchi et al. 2009)<ref>PMID:19697358 </ref>.

==References==
<references />

Group:MUZIC:Synaptopodin

2013-02-08T17:39:41Z

Eduardo Bezerra: /* Sequence annotation */

== Introduction ==

Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes and in muscle cells is exclusively expressed in terminally differentiated skeletal muscle cells, where is colocalized with alpha-actinin and filamin C in the Z-disc. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.

== Sequence annotation ==

The protein KIBRA localized in podocytes directly bind to synaptopodin via the WW domains. The long variant of synaptopodin (903 aa) that is expressed in podocytes contains two internal PPxY sites, two PEST sequences, an actin-binding domain, and four α-actinin–binding regions (Duning et al. 2008)<ref>PMID: 18596123</ref>.

[[Image:Synaptopodin_isoforms.png|700px|left|thumb|Synaptopodin exist in three different isoforms produced by alternative splicing of the N- and C-terminal exons.]]

== Structure ==
There is no structure related for this protein.

== Function and interactions ==

The high degree of sequence similarity between the three members of the podin family in defined regions suggests analog binding properties. Indeed, biochemical studies revealed that all podin proteins interact with the Ig-domains 20-21 of filamin C. Similar to the situation in synaptopodin interaction studies showed that alpha-actinin binds also myopodin and tritopodin at multiple binding sites.(Linnemann et al. 2010)<ref>PMID:20554076</ref>.Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

Members of the podin family have been implicated in cancers. Synaptopodin 2 (myopodin) is expressed primarily in nuclei of proliferating myoblast cells. Cytoplasmic Synaptopodin 2 appears within hours of differentiation of myoblasts into myotubes and is found in Z-lines of mature myotubes (Weins et al. 2001)<ref>PMID:11673475 </ref>.
There is another level of complexity regarding the role of actin bundling proteins in cancer. Metastasis requires cell motility, a property normally associated with plasticity of actin filaments. However, there is ample evidence that bundling of actin filaments is a prerequisite for formation of invadosomes. Elevated levels of some actin bundling proteins are associated with more aggressive cancer phenotypes.(Iguchi et al. 2009)<ref>PMID:19697358 </ref>.

==References==
<references />

Group:MUZIC:Synaptopodin

2013-02-08T17:35:54Z

Eduardo Bezerra: /* Sequence annotation */

== Introduction ==

Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes and in muscle cells is exclusively expressed in terminally differentiated skeletal muscle cells, where is colocalized with alpha-actinin and filamin C in the Z-disc. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.

== Sequence annotation ==

The protein KIBRA localized in podocytes directly bind to synaptopodin via the WW domains. The long variant of synaptopodin (903 aa) that is expressed in podocytes contains two internal PPxY sites, two PEST sequences, an actin-binding domain, and four α-actinin–binding regions.

[[Image:Synaptopodin_isoforms.png|700px|left|thumb|Synaptopodin exist in three different isoforms produced by alternative splicing of the N- and C-terminal exons.]]

== Structure ==
There is no structure related for this protein.

== Function and interactions ==

The high degree of sequence similarity between the three members of the podin family in defined regions suggests analog binding properties. Indeed, biochemical studies revealed that all podin proteins interact with the Ig-domains 20-21 of filamin C. Similar to the situation in synaptopodin interaction studies showed that alpha-actinin binds also myopodin and tritopodin at multiple binding sites.(Linnemann et al. 2010)<ref>PMID:20554076</ref>.Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

Members of the podin family have been implicated in cancers. Synaptopodin 2 (myopodin) is expressed primarily in nuclei of proliferating myoblast cells. Cytoplasmic Synaptopodin 2 appears within hours of differentiation of myoblasts into myotubes and is found in Z-lines of mature myotubes (Weins et al. 2001)<ref>PMID:11673475 </ref>.
There is another level of complexity regarding the role of actin bundling proteins in cancer. Metastasis requires cell motility, a property normally associated with plasticity of actin filaments. However, there is ample evidence that bundling of actin filaments is a prerequisite for formation of invadosomes. Elevated levels of some actin bundling proteins are associated with more aggressive cancer phenotypes.(Iguchi et al. 2009)<ref>PMID:19697358 </ref>.

==References==
<references />

Group:MUZIC:Synaptopodin

2013-02-08T17:35:40Z

Eduardo Bezerra: /* Sequence annotation */

== Introduction ==

Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes and in muscle cells is exclusively expressed in terminally differentiated skeletal muscle cells, where is colocalized with alpha-actinin and filamin C in the Z-disc. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.

== Sequence annotation ==

fThe protein KIBRA localized in podocytes directly bind to synaptopodin via the WW domains. The long variant of synaptopodin (903 aa) that is expressed in podocytes contains two internal PPxY sites, two PEST sequences, an actin-binding domain, and four α-actinin–binding regions.gh

[[Image:Synaptopodin_isoforms.png|700px|left|thumb|Synaptopodin exist in three different isoforms produced by alternative splicing of the N- and C-terminal exons.]]

fgh

== Structure ==
There is no structure related for this protein.

== Function and interactions ==

The high degree of sequence similarity between the three members of the podin family in defined regions suggests analog binding properties. Indeed, biochemical studies revealed that all podin proteins interact with the Ig-domains 20-21 of filamin C. Similar to the situation in synaptopodin interaction studies showed that alpha-actinin binds also myopodin and tritopodin at multiple binding sites.(Linnemann et al. 2010)<ref>PMID:20554076</ref>.Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

Members of the podin family have been implicated in cancers. Synaptopodin 2 (myopodin) is expressed primarily in nuclei of proliferating myoblast cells. Cytoplasmic Synaptopodin 2 appears within hours of differentiation of myoblasts into myotubes and is found in Z-lines of mature myotubes (Weins et al. 2001)<ref>PMID:11673475 </ref>.
There is another level of complexity regarding the role of actin bundling proteins in cancer. Metastasis requires cell motility, a property normally associated with plasticity of actin filaments. However, there is ample evidence that bundling of actin filaments is a prerequisite for formation of invadosomes. Elevated levels of some actin bundling proteins are associated with more aggressive cancer phenotypes.(Iguchi et al. 2009)<ref>PMID:19697358 </ref>.

==References==
<references />

Group:MUZIC:Synaptopodin

2013-02-08T17:35:22Z

Eduardo Bezerra: /* Sequence annotation */

== Introduction ==

Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes and in muscle cells is exclusively expressed in terminally differentiated skeletal muscle cells, where is colocalized with alpha-actinin and filamin C in the Z-disc. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.

== Sequence annotation ==

fgh

[[Image:Synaptopodin_isoforms.png|700px|left|thumb|Synaptopodin exist in three different isoforms produced by alternative splicing of the N- and C-terminal exons.]]

fgh

== Structure ==
There is no structure related for this protein.

== Function and interactions ==

The high degree of sequence similarity between the three members of the podin family in defined regions suggests analog binding properties. Indeed, biochemical studies revealed that all podin proteins interact with the Ig-domains 20-21 of filamin C. Similar to the situation in synaptopodin interaction studies showed that alpha-actinin binds also myopodin and tritopodin at multiple binding sites.(Linnemann et al. 2010)<ref>PMID:20554076</ref>.Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

Members of the podin family have been implicated in cancers. Synaptopodin 2 (myopodin) is expressed primarily in nuclei of proliferating myoblast cells. Cytoplasmic Synaptopodin 2 appears within hours of differentiation of myoblasts into myotubes and is found in Z-lines of mature myotubes (Weins et al. 2001)<ref>PMID:11673475 </ref>.
There is another level of complexity regarding the role of actin bundling proteins in cancer. Metastasis requires cell motility, a property normally associated with plasticity of actin filaments. However, there is ample evidence that bundling of actin filaments is a prerequisite for formation of invadosomes. Elevated levels of some actin bundling proteins are associated with more aggressive cancer phenotypes.(Iguchi et al. 2009)<ref>PMID:19697358 </ref>.

==References==
<references />

Group:MUZIC:Synaptopodin

2013-02-08T17:34:52Z

Eduardo Bezerra: /* Sequence annotation */

== Introduction ==

Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes and in muscle cells is exclusively expressed in terminally differentiated skeletal muscle cells, where is colocalized with alpha-actinin and filamin C in the Z-disc. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.

== Sequence annotation ==
The protein KIBRA localized in podocytes directly bind to synaptopodin via the WW domains. The long variant of synaptopodin (903 aa) that is expressed in podocytes contains two internal PPxY sites, two PEST sequences, an actin-binding domain, and four α-actinin–binding regions.

[[Image:Synaptopodin_isoforms.png|700px|left|thumb|Synaptopodin exist in three different isoforms produced by alternative splicing of the N- and C-terminal exons.]]

== Structure ==
There is no structure related for this protein.

== Function and interactions ==

The high degree of sequence similarity between the three members of the podin family in defined regions suggests analog binding properties. Indeed, biochemical studies revealed that all podin proteins interact with the Ig-domains 20-21 of filamin C. Similar to the situation in synaptopodin interaction studies showed that alpha-actinin binds also myopodin and tritopodin at multiple binding sites.(Linnemann et al. 2010)<ref>PMID:20554076</ref>.Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

Members of the podin family have been implicated in cancers. Synaptopodin 2 (myopodin) is expressed primarily in nuclei of proliferating myoblast cells. Cytoplasmic Synaptopodin 2 appears within hours of differentiation of myoblasts into myotubes and is found in Z-lines of mature myotubes (Weins et al. 2001)<ref>PMID:11673475 </ref>.
There is another level of complexity regarding the role of actin bundling proteins in cancer. Metastasis requires cell motility, a property normally associated with plasticity of actin filaments. However, there is ample evidence that bundling of actin filaments is a prerequisite for formation of invadosomes. Elevated levels of some actin bundling proteins are associated with more aggressive cancer phenotypes.(Iguchi et al. 2009)<ref>PMID:19697358 </ref>.

==References==
<references />

File:Synaptopodin isoforms.png

2013-02-08T15:41:28Z

Eduardo Bezerra: uploaded a new version of "Image:Synaptopodin isoforms.png": Synaptopodin exist in three different isoforms produced by alternative splicing of the N- and C-terminal exons.

Group:MUZIC:Synaptopodin

2013-02-05T16:36:00Z

Eduardo Bezerra: /* Sequence annotation */

== Introduction ==

Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes and in muscle cells is exclusively expressed in terminally differentiated skeletal muscle cells, where is colocalized with alpha-actinin and filamin C in the Z-disc. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.

== Sequence annotation ==

[[Image:Synaptopodin_isoforms.png|700px|left|thumb|Synaptopodin exist in three different isoforms produced by alternative splicing of the N- and C-terminal exons.]]

== Structure ==
There is no structure related for this protein.

== Function and interactions ==

The high degree of sequence similarity between the three members of the podin family in defined regions suggests analog binding properties. Indeed, biochemical studies revealed that all podin proteins interact with the Ig-domains 20-21 of filamin C. Similar to the situation in synaptopodin interaction studies showed that alpha-actinin binds also myopodin and tritopodin at multiple binding sites.(Linnemann et al. 2010)<ref>PMID:20554076</ref>.Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

Members of the podin family have been implicated in cancers. Synaptopodin 2 (myopodin) is expressed primarily in nuclei of proliferating myoblast cells. Cytoplasmic Synaptopodin 2 appears within hours of differentiation of myoblasts into myotubes and is found in Z-lines of mature myotubes (Weins et al. 2001)<ref>PMID:11673475 </ref>.
There is another level of complexity regarding the role of actin bundling proteins in cancer. Metastasis requires cell motility, a property normally associated with plasticity of actin filaments. However, there is ample evidence that bundling of actin filaments is a prerequisite for formation of invadosomes. Elevated levels of some actin bundling proteins are associated with more aggressive cancer phenotypes.(Iguchi et al. 2009)<ref>PMID:19697358 </ref>.

==References==
<references />

Group:MUZIC:Synaptopodin

2013-02-05T16:34:06Z

Eduardo Bezerra: /* Sequence annotation */

== Introduction ==

Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes and in muscle cells is exclusively expressed in terminally differentiated skeletal muscle cells, where is colocalized with alpha-actinin and filamin C in the Z-disc. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.

== Sequence annotation ==

[[Image:Synaptopodin_isoforms.png|700px|left|thumb|Synaptopodin isoforms]]

== Structure ==
There is no structure related for this protein.

== Function and interactions ==

The high degree of sequence similarity between the three members of the podin family in defined regions suggests analog binding properties. Indeed, biochemical studies revealed that all podin proteins interact with the Ig-domains 20-21 of filamin C. Similar to the situation in synaptopodin interaction studies showed that alpha-actinin binds also myopodin and tritopodin at multiple binding sites.(Linnemann et al. 2010)<ref>PMID:20554076</ref>.Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

Members of the podin family have been implicated in cancers. Synaptopodin 2 (myopodin) is expressed primarily in nuclei of proliferating myoblast cells. Cytoplasmic Synaptopodin 2 appears within hours of differentiation of myoblasts into myotubes and is found in Z-lines of mature myotubes (Weins et al. 2001)<ref>PMID:11673475 </ref>.
There is another level of complexity regarding the role of actin bundling proteins in cancer. Metastasis requires cell motility, a property normally associated with plasticity of actin filaments. However, there is ample evidence that bundling of actin filaments is a prerequisite for formation of invadosomes. Elevated levels of some actin bundling proteins are associated with more aggressive cancer phenotypes.(Iguchi et al. 2009)<ref>PMID:19697358 </ref>.

==References==
<references />

File:Synaptopodin isoforms.png

2013-02-05T16:32:30Z

Eduardo Bezerra: uploaded a new version of "Image:Synaptopodin isoforms.png": Synaptopodin exist in three different isoforms produced by alternative splicing of the N- and C-terminal exons.

Group:MUZIC:Synaptopodin

2013-01-17T16:51:23Z

Eduardo Bezerra: /* Pathology */

== Introduction ==

Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes and in muscle cells is exclusively expressed in terminally differentiated skeletal muscle cells, where is colocalized with alpha-actinin and filamin C in the Z-disc. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.

== Sequence annotation ==

[[Image:Synaptopodin isoform.png|700px|left|thumb|Synaptopodin isoforms]]

== Structure ==
There is no structure related for this protein.

== Function and interactions ==

The high degree of sequence similarity between the three members of the podin family in defined regions suggests analog binding properties. Indeed, biochemical studies revealed that all podin proteins interact with the Ig-domains 20-21 of filamin C. Similar to the situation in synaptopodin interaction studies showed that alpha-actinin binds also myopodin and tritopodin at multiple binding sites.(Linnemann et al. 2010)<ref>PMID:20554076</ref>.Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

Members of the podin family have been implicated in cancers. Synaptopodin 2 (myopodin) is expressed primarily in nuclei of proliferating myoblast cells. Cytoplasmic Synaptopodin 2 appears within hours of differentiation of myoblasts into myotubes and is found in Z-lines of mature myotubes (Weins et al. 2001)<ref>PMID:11673475 </ref>.
There is another level of complexity regarding the role of actin bundling proteins in cancer. Metastasis requires cell motility, a property normally associated with plasticity of actin filaments. However, there is ample evidence that bundling of actin filaments is a prerequisite for formation of invadosomes. Elevated levels of some actin bundling proteins are associated with more aggressive cancer phenotypes.(Iguchi et al. 2009)<ref>PMID:19697358 </ref>.

==References==
<references />

Group:MUZIC:Synaptopodin

2013-01-17T16:46:15Z

Eduardo Bezerra: /* Pathology */

== Introduction ==

Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes and in muscle cells is exclusively expressed in terminally differentiated skeletal muscle cells, where is colocalized with alpha-actinin and filamin C in the Z-disc. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.

== Sequence annotation ==

[[Image:Synaptopodin isoform.png|700px|left|thumb|Synaptopodin isoforms]]

== Structure ==
There is no structure related for this protein.

== Function and interactions ==

The high degree of sequence similarity between the three members of the podin family in defined regions suggests analog binding properties. Indeed, biochemical studies revealed that all podin proteins interact with the Ig-domains 20-21 of filamin C. Similar to the situation in synaptopodin interaction studies showed that alpha-actinin binds also myopodin and tritopodin at multiple binding sites.(Linnemann et al. 2010)<ref>PMID:20554076</ref>.Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

Members of the podin family have been implicated in cancers. Synaptopodin 2 (myopodin) is expressed primarily in nuclei of proliferating myoblast cells. Cytoplasmic Synaptopodin 2 appears within hours of differentiation of myoblasts into myotubes and is found in Z-lines of mature myotubes (Weins et al. 2001)<ref>PMID:11673475 </ref>.

==References==
<references />

Group:MUZIC:Synaptopodin

2013-01-17T16:45:18Z

Eduardo Bezerra: /* Pathology */

== Introduction ==

Synaptopodin, a protein encoded by the gene [http://www.uniprot.org/uniprot/Q8N3V7 SYNPO],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes and in muscle cells is exclusively expressed in terminally differentiated skeletal muscle cells, where is colocalized with alpha-actinin and filamin C in the Z-disc. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref>. Synaptopodin is either a member of the podin family, where we can find [http://proteopedia.org/wiki/index.php?title=User:Irela_Gretchen_Reza_Mazar/Workbench/Myopodin myopodin], present in avian smooth muscle (Leinweber et al. 1999)<ref> PMID:10555072</ref> heart and skeletal muscle (myopodin, genethonin-2, synaptopodin 2 or fesselin) (Weins et al. 2001)<ref>PMID:11673475 </ref>, and also the third member of the synaptopodin family of proteins, the synaptopodin 2-like protein is found in heart and skeletal muscle tissue and is better known under the names [http://www.proteopedia.org/wiki/index.php/User:Irela_Gretchen_Reza_Mazar/Workbench/Tritopodin tritopodin] (Claeys et al. 2009)<ref>PMID:19151983</ref> or CHAP (Beqqali et al. 2010)<ref>PMID:20215401</ref>.

== Sequence annotation ==

[[Image:Synaptopodin isoform.png|700px|left|thumb|Synaptopodin isoforms]]

== Structure ==
There is no structure related for this protein.

== Function and interactions ==

The high degree of sequence similarity between the three members of the podin family in defined regions suggests analog binding properties. Indeed, biochemical studies revealed that all podin proteins interact with the Ig-domains 20-21 of filamin C. Similar to the situation in synaptopodin interaction studies showed that alpha-actinin binds also myopodin and tritopodin at multiple binding sites.(Linnemann et al. 2010)<ref>PMID:20554076</ref>.Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

Members of the podin family have been implicated in cancers. Synaptopodin 2 (myopodin) is expressed primarily in nuclei of proliferating myoblast cells. Cytoplasmic Synaptopodin 2 appears within hours of differentiation of myoblasts into myotubes and is found in Z-lines of mature myotubes (Weins et al. 2001).

==References==
<references />

Group:MUZIC:Synaptopodin

2013-01-17T15:21:09Z

Eduardo Bezerra: /* Introduction */

Group:MUZIC:Synaptopodin

2013-01-17T15:15:34Z

Eduardo Bezerra: /* Function and interactions */

Group:MUZIC:Synaptopodin

2013-01-17T15:12:18Z

Eduardo Bezerra: /* Introduction */

Group:MUZIC:Synaptopodin

2013-01-17T15:09:28Z

Eduardo Bezerra: /* Introduction */

Group:MUZIC:Synaptopodin

2013-01-17T15:07:13Z

Eduardo Bezerra: /* Sequence annotation */

Group:MUZIC:Synaptopodin

2013-01-17T15:06:25Z

Eduardo Bezerra: /* Introduction */

Group:MUZIC:Synaptopodin

2013-01-16T18:13:39Z

Eduardo Bezerra: /* Function and interactions */

Group:MUZIC:Synaptopodin

2013-01-16T18:08:57Z

Eduardo Bezerra: /* Function and interactions */

Group:MUZIC:Synaptopodin

2013-01-16T18:04:55Z

Eduardo Bezerra: /* Function and interactions */

Group:MUZIC:Synaptopodin

2013-01-16T17:59:27Z

Eduardo Bezerra: /* Introduction */

Group:MUZIC:Synaptopodin

2013-01-16T17:56:51Z

Eduardo Bezerra: /* Introduction */

Group:MUZIC:Synaptopodin

2013-01-16T17:55:32Z

Eduardo Bezerra: /* Introduction */

Group:MUZIC:Synaptopodin

2013-01-16T17:47:54Z

Eduardo Bezerra: /* Introduction */

Group:MUZIC:Synaptopodin

2013-01-16T17:46:26Z

Eduardo Bezerra: /* Introduction */

Group:MUZIC:Synaptopodin

2011-07-11T14:48:37Z

Eduardo Bezerra:

Group:MUZIC:Synaptopodin

2011-07-11T14:33:42Z

Eduardo Bezerra:

Group:MUZIC:Synaptopodin

2011-07-11T14:23:21Z

Eduardo Bezerra:

Group:MUZIC:Synaptopodin

2011-07-11T14:07:57Z

Eduardo Bezerra:

== Introduction ==

Synaptopodin, a protein encoded by the gene SYNPO [http://www.uniprot.org/uniprot/Q8N3V7],and represents a novel kind of proline-rich, actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and podocyte foot processes. Either the founding member of a novel class of actin-associated proteins and also expressed in the brain, where it is found at the postsynaptic density and the spine apparatus in a subset of telencephalic neurons. In both brain and kidney, in vivo and in vitro, synaptopodin gene expression is differentiation dependent <ref>PMID: 9314539</ref> <ref>PMID:10701442</ref> and have no significant homology to any known protein except myopodin, the second member of the gene family<ref>PMID:11673475</ref>.

== Sequence annotation ==

[[Image:Synaptopodin isoform.png|700px]]

== Structure ==

== Function and interactions ==

Synaptopodin seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity.
Synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration <ref>PMID:16622418</ref>. Postictal upregulation of Synaptopodin mRNA levels in target cell populations of limbic epilepsy-elicited damage and subsequent Synaptopodin protein expression largely co-localized with remodeling processes as demonstrated by mossy fiber sprouting <ref>PMID:11303792</ref>.

== Pathology ==

==References==
<references />

File:Filamin C interaction 2.PNG

2011-07-11T13:58:51Z

Eduardo Bezerra:

File:Podin family iso.PNG

2011-07-11T13:47:32Z

Eduardo Bezerra: