Proteopedia - User contributions [en]

Group:MUZIC:Myotilin

2011-12-09T13:13:36Z

Denisa Mullerova:

'''
== Introduction ==
'''

Myotilin is a 498-amino-acid cytoskeletal protein with the size of 57 kDa, localized in sarcomeric Z-discs of both skeletal and cardiac muscle<ref>PMID:10369880</ref>. It consists of a unique serine-rich amino-terminus, two Ig-domains and a short carboxy-terminus with a PDZ-binding motif [http://www.uniprot.org/uniprot/Q9UBF9 (UNIPROT Myotilin)]. Myotilin belongs to a small group of scaffolding proteins, together with palladin and myopapalladin, which regulate actin organisation<ref>PMID:16164966</ref> but was also found to interact with several other sarcomeric proteins.<ref>PMID:19418025</ref> <ref>PMID:11038172</ref> <ref>PMID:16076904</ref> Muscle disorders such as limb-girdle muscular dystrophy type 1A and myofibrillar myopathy (MFM) have been linked to point mutations in myotilin.<ref>PMID:17074808</ref>

== Pathology ==

The disorders typically manifest as proximal weakness of the extremities but may also include cardiomyopathy and peripheral neuropathy. Ultrastructural changes include Z-disk alterations and accumulation of dense filamentous myotilin. Single missense mutation, mostly in the N-terminal serine-rich part of the protein, causes the onset of both disorders. Thus, mutation has a dominant negative effect on functionality of myotilin.<ref>PMID:10958653</ref> <ref>PMID:19181098</ref>

== Interactions of Myotilin ==

All myotilin's binding partners are components of Z-disk and include actin,<ref>PMID:16122733</ref> α-actinin,<ref>PMID:10369880</ref> filamins, FATZ<ref>PMID:16076904</ref> and ZASP<ref>PMID:19047374</ref>. Myotilin cross-links and efficiently bundles actin filaments.<ref>PMID:12499399</ref>

<Structure load='2KDG' size='250' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='250' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'/>

== References ==

<references/>

Group:MUZIC:Myotilin

2011-12-09T13:12:43Z

Denisa Mullerova:

'''
== Introduction ==
'''

Myotilin is a 498-amino-acid cytoskeletal protein with the size of 57 kDa, localized in sarcomeric Z-discs of both skeletal and cardiac muscle<ref>PMID:10369880</ref>. It consists of a unique serine-rich amino-terminus, two Ig-domains and a short carboxy-terminus with a PDZ-binding motif [http://www.uniprot.org/uniprot/Q9UBF9 (UNIPROT Myotilin)]. Myotilin belongs to a small group of scaffolding proteins, together with palladin and myopapalladin, which regulate actin organisation<ref>PMID:16164966</ref> but was also found to interact with several other sarcomeric proteins<ref>PMID:19418025</ref> <ref>PMID:11038172</ref> <ref>PMID:16076904</ref>. Muscle disorders such as limb-girdle muscular dystrophy type 1A and myofibrillar myopathy (MFM) have been linked to point mutations in myotilin.<ref>PMID:17074808</ref>

== Pathology ==

The disorders typically manifest as proximal weakness of the extremities but may also include cardiomyopathy and peripheral neuropathy. Ultrastructural changes include Z-disk alterations and accumulation of dense filamentous myotilin. Single missense mutation, mostly in the N-terminal serine-rich part of the protein, causes the onset of both disorders. Thus, mutation has a dominant negative effect on functionality of myotilin.<ref>PMID:10958653</ref> <ref>PMID:19181098</ref>

== Interactions of Myotilin ==

All myotilin's binding partners are components of Z-disk and include actin,<ref>PMID:16122733</ref> α-actinin,<ref>PMID:10369880</ref> filamins, FATZ<ref>PMID:16076904</ref> and ZASP<ref>PMID:19047374</ref>. Myotilin cross-links and efficiently bundles actin filaments.<ref>PMID:12499399</ref>

<Structure load='2KDG' size='250' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='250' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'/>

== References ==

<references/>

Group:MUZIC:Myotilin

2011-12-09T13:10:49Z

Denisa Mullerova:

'''
== Introduction ==
'''

Myotilin is a cytoskeletal protein with the size of 57 kDa, localized in sarcomeric Z-discs of both skeletal and cardiac muscle <ref>PMID:10369880</ref>. It consists of a unique serine-rich amino-terminus, two Ig-domains and a short carboxy-terminus with a PDZ-binding motif [http://www.uniprot.org/uniprot/Q9UBF9 (UNIPROT Myotilin)]. Myotilin belongs to a small group of scaffolding proteins, together with palladin and myopapalladin, which regulate actin organisation <ref>PMID:16164966</ref> but was also found to interact with several other sarcomeric proteins <ref>PMID:19418025</ref> <ref>PMID:11038172</ref> <ref>PMID:16076904</ref>. Muscle disorders such as limb-girdle muscular dystrophy type 1A and myofibrillar myopathy (MFM) have been linked to point mutations in myotilin <ref>PMID:17074808</ref>.

== Pathology ==

The disorders typically manifest as proximal weakness of the extremities but may also include cardiomyopathy and peripheral neuropathy. Ultrastructural changes include Z-disk alterations and accumulation of dense filamentous myotilin. Single missense mutation, mostly in the N-terminal serine-rich part of the protein, causes the onset of both disorders. Thus, mutation has a dominant negative effect on functionality of myotilin <ref>PMID:10958653</ref> <ref>PMID:19181098</ref>.

== Interactions of Myotilin ==

All myotilin's binding partners are components of Z-disk and include actin, <ref>PMID:16122733</ref> α-actinin, <ref>PMID:10369880</ref> filamins, FATZ <ref>PMID:16076904</ref> and ZASP <ref>PMID:19047374</ref>. Myotilin cross-links and efficiently bundles actin filaments <ref>PMID:12499399</ref>.

<Structure load='2KDG' size='250' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='250' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'/>

== References ==

<references/>

Group:MUZIC:Myotilin

2011-12-09T13:08:52Z

Denisa Mullerova:

'''
== Introduction ==
'''

Myotilin is a cytoskeletal protein with the size of 57 kDa, localized in sarcomeric Z-discs of both skeletal and cardiac muscle <ref>PMID:10369880</ref>. It consists of a unique serine-rich amino-terminus, two Ig-domains and a short carboxy-terminus with a PDZ-binding motif [http://www.uniprot.org/uniprot/Q9UBF9 (UNIPROT Myotilin)]. Myotilin belongs to a small group of scaffolding proteins, together with palladin and myopapalladin, which regulate actin organisation <ref>PMID:16164966</ref> but was also found to interact with several other sarcomeric proteins <ref>PMID:19418025</ref> <ref>PMID:11038172</ref> <ref>PMID:16076904</ref>. Muscle disorders such as limb-girdle muscular dystrophy type 1A and myofibrillar myopathy (MFM) have been linked to point mutations in myotilin <ref>PMID:17074808</ref>.

== Pathology ==

The disorders typically manifest as proximal weakness of the extremities but may also include cardiomyopathy and peripheral neuropathy. Ultrastructural changes include Z-disk alterations and accumulation of dense filamentous myotilin. Single missense mutation, mostly in the N-terminal serine-rich part of the protein, causes the onset of both disorders. Thus, mutation has a dominant negative effect on functionality of myotilin <ref>PMID:10958653</ref> <ref>PMID:19181098</ref>.

== Interactions of Myotilin ==

All myotilin's binding partners are components of Z-disk and include actin <ref>PMID:16122733</ref> , α-actinin <ref>PMID:10369880</ref>, filamins, FATZ <ref>PMID:16076904</ref> and ZASP <ref>PMID:19047374</ref>. Myotilin cross-links and efficiently bundles actin filaments <ref>PMID:12499399</ref>.

<Structure load='2KDG' size='250' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='250' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'/>

== References ==

<references/>

Group:MUZIC:Myotilin

2011-12-09T13:06:35Z

Denisa Mullerova:

'''
== Introduction ==
'''

Myotilin is a cytoskeletal protein with the size of 57 kDa, localized in sarcomeric Z-discs of both skeletal and cardiac muscle <ref>PMID:10369880</ref>. It consists of a unique serine-rich amino-terminus, two Ig-domains and a short carboxy-terminus with a PDZ-binding motif [http://www.uniprot.org/uniprot/Q9UBF9 (UNIPROT Myotilin)]. Myotilin belongs to a small group of scaffolding proteins, together with palladin and myopapalladin, which regulate actin organisation <ref>PMID:16164966</ref> but was also found to interact with several other sarcomeric proteins <ref>PMID:19418025</ref> <ref>PMID:11038172</ref> <ref>PMID:16076904</ref>. Muscle disorders such as limb-girdle muscular dystrophy type 1A and myofibrillar myopathy (MFM) have been linked to point mutations in myotilin <ref>PMID:17074808</ref>.

== Pathology ==

The disorders typically manifest as proximal weakness of the extremities but may also include cardiomyopathy and peripheral neuropathy. Ultrastructural changes include Z-disk alterations and accumulation of dense filamentous myotilin. Single missense mutation, mostly in the N-terminal serine-rich part of the protein, causes the onset of both disorders. Thus, mutation has a dominant negative effect on functionality of myotilin <ref>PMID:10958653</ref> <ref>PMID:19181098</ref>.

== Interactions of Myotilin ==

All myotilin's binding partners are components of Z-disk and include actin <ref>PMID:16122733</ref> , α-actinin <ref>PMID:10369880</ref>, filamins, FATZ <ref>PMID:16076904</ref> and ZASP <ref>PMID:19047374</ref>. Myotilin cross-links and efficiently bundles actin filaments.

<Structure load='2KDG' size='250' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='250' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'/>

== References ==

<references/>

Group:MUZIC:Myotilin

2011-12-09T12:39:47Z

Denisa Mullerova:

'''
== Introduction ==
'''

Myotilin is a cytoskeletal protein with the size of 57 kDa, localized in sarcomeric Z-discs of both skeletal and cardiac muscle <ref>PMID:10369880</ref>. It consists of a unique serine-rich amino-terminus, two Ig-domains and a short carboxy-terminus with a PDZ-binding motif [http://www.uniprot.org/uniprot/Q9UBF9 (UNIPROT Myotilin)]. Myotilin belongs to a small group of scaffolding proteins, together with palladin and myopapalladin, which regulate actin organisation <ref>PMID:16164966</ref> but was also found to interact with several other sarcomeric proteins like actin, α-actinin, filamin C <ref>PMID:19418025</ref> <ref>PMID:11038172</ref> and FATZ-1/FATZ-2 <ref>PMID:16076904</ref>. Muscle disorders such as limb-girdle muscular dystrophy type 1A and myofibrillar myopathy (MFM) have been linked to point mutations in myotilin <ref>PMID:17074808</ref>.

== Pathology ==

The disorders typically manifest as proximal weakness of the extremities but may also include cardiomyopathy and peripheral neuropathy. Ultrastructural changes include Z-disk alterations and accumulation of dense filamentous myotilin. Single missense mutation, mostly in the N-terminal serine-rich part of the protein, causes the onset of both disorders. Thus, mutation has a dominant negative effect on functionality of myotilin <ref>PMID:10958653</ref> <ref>PMID:19181098</ref>.

== Interactions of Myotilin ==

<Structure load='2KDG' size='250' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='250' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'/>

== References ==

<references/>

Group:MUZIC:Myotilin

2011-12-09T12:35:52Z

Denisa Mullerova:

'''
== Introduction ==
'''

Myotilin is a cytoskeletal protein with the size of 57 kDa, localized in sarcomeric Z-discs of both skeletal and cardiac muscle <ref>PMID:10369880</ref>. It consists of a unique serine-rich amino-terminus, two Ig-domains and a short carboxy-terminus with a PDZ-binding motif [http://www.uniprot.org/uniprot/Q9UBF9 (UNIPROT Myotilin)]. Myotilin belongs to a small group of scaffolding proteins, together with palladin and myopapalladin, which regulate actin organisation <ref>PMID:16164966</ref> but was also found to interact with several other sarcomeric proteins like actin, α-actinin, filamin C <ref>PMID:19418025</ref><ref>PMID:11038172</ref> and FATZ-1/FATZ-2 <ref>PMID:16076904</ref>. Muscle disorders such as limb-girdle muscular dystrophy type 1A and myofibrillar myopathy (MFM) have been linked to point mutations in myotilin <ref>PMID:17074808</ref>.

== Pathology ==

The disorders typically manifest as proximal weakness of the extremities but may also include cardiomyopathy and peripheral neuropathy. Ultrastructural changes include Z-disk alterations and accumulation of dense filamentous myotilin. Single missense mutation, mostly in the N-terminal serine-rich part of the protein, causes the onset of both disorders. Thus, mutation has a dominant negative effect on functionality of myotilin <ref>PMID:10958653</ref> <ref>PMID:19181098</ref>.

<Structure load='2KDG' size='250' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='250' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'/>

== References ==

<references/>

Group:MUZIC:Myotilin

2011-10-14T12:48:02Z

Denisa Mullerova:

Group:MUZIC:Myotilin

2011-07-18T15:04:14Z

Denisa Mullerova:

Group:MUZIC:Myotilin

2011-07-18T15:00:02Z

Denisa Mullerova:

Group:MUZIC:Myotilin

2011-07-18T14:20:36Z

Denisa Mullerova:

Group:MUZIC:Myotilin

2011-07-18T14:14:13Z

Denisa Mullerova:

Group:MUZIC:Myotilin

2011-07-18T14:12:34Z

Denisa Mullerova: /* Myotilin */

User:Denisa Mullerova

2011-07-12T09:33:06Z

Denisa Mullerova:

postdoc at Evitra AB Stockholm, Sweden

User:Denisa Mullerova

2011-07-12T09:32:25Z

Denisa Mullerova:

postdoc at Evitra AB Stockholm, Sweden
prof. Par Nordlund's lab

Group:MUZIC:Myotilin

2011-06-24T08:27:30Z

Denisa Mullerova:

'''
== Myotilin ==
'''

Myotilin is a cytoskeletal protein with the size of 57 kDa, localized in sarcomeric Z-discs of both skeletal and cardiac muscle <ref>PMID:10369880</ref>. It consists of a unique serine-rich amino-terminus, two Ig-domains and a short carboxy-terminus with a PDZ-binding motif. Myotilin belongs to a small group of scaffolding proteins, together with palladin and myopapalladin, which regulate actin organisation <ref>PMID:16164966</ref> but was also found to interact with several other sarcomeric proteins like actin, a-actinin, filamin C <ref>PMID:19418025</ref><ref>PMID:11038172</ref> and FATZ-1/FATZ-2 <ref>PMID:16076904</ref>. Muscle disorders such as limb-girdle muscular dystrophy type 1A and myofibrillar myopathy have been linked to point mutations in myotilin <ref>PMID:17074808</ref>.

'''Uniprot''' Q9UBF9
[http://www.uniprot.org/uniprot/Q9UBF9]

<Structure load='2KDG' size='250' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='250' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'/>

'''References'''
<references/>

Group:MUZIC:Myotilin

2011-06-24T08:25:50Z

Denisa Mullerova:

'''
== Myotilin ==
'''

Myotilin is a cytoskeletal protein with the size of 57 kDa, localized in sarcomeric Z-discs of both skeletal and cardiac muscle <ref>PMID:10369880</ref>. It consists of a unique serine-rich amino-terminus, two Ig-domains and a short carboxy-terminus with a PDZ-binding motif. Myotilin belongs to a small group of scaffolding proteins, together with palladin and myopapalladin, which regulate actin organisation <ref>PMID:16164966</ref> but was also found to interact with several other sarcomeric proteins like actin, a-actinin, filamin C <ref>PMID:19418025</ref>, <ref>PMID:11038172</ref> and FATZ-1/FATZ-2 <ref>PMID:16076904</ref>. Muscle disorders such as limb-girdle muscular dystrophy type 1A and myofibrillar myopathy have been linked to point mutations in myotilin <ref>PMID:17074808</ref>.

'''Uniprot''' Q9UBF9
[http://www.uniprot.org/uniprot/Q9UBF9]

<Structure load='2KDG' size='250' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='250' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'/>

'''References'''
<references/>

Group:MUZIC:Myotilin

2011-06-23T16:16:48Z

Denisa Mullerova:

'''
== Myotilin ==
'''

Myotilin is a 57 kDa cytoskeletal protein containing a unique N-terminal region and a
C-terminal region that contains two Ig-like domains homologous
to the Ig-like domains 7 and 8 of titin <ref>PMID:11699871</ref>.

'''Uniprot''' Q9UBF9
[http://www.uniprot.org/uniprot/Q9UBF9]

<Structure load='2KDG' size='250' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='250' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'/>

'''References'''
<references/>

Group:MUZIC:Myotilin

2011-06-23T16:15:34Z

Denisa Mullerova:

Group:MUZIC:Myotilin

2011-06-23T16:11:16Z

Denisa Mullerova:

Group:MUZIC:Myotilin

2011-06-23T16:07:16Z

Denisa Mullerova:

'''
== Myotilin ==
'''

Myotilin is a 57 kDa cytoskeletal protein containing a unique N-terminal region and a
C-terminal region that contains two Ig-like domains homologous
to the Ig-like domains 7 and 8 of titin <ref name="PMID:11699871">Telethonin and other new proteins of the Z-disc of skeletal muscle.</ref>.

'''Uniprot''' Q9UBF9
[http://www.uniprot.org/uniprot/Q9UBF9]

<Structure load='2KDG' size='250' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='250' frame='true' align='left' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'>

'''References'''
<references />

Group:MUZIC:Myotilin

2011-06-23T16:04:30Z

Denisa Mullerova:

'''
== Myotilin ==
'''

Myotilin is a 57 kDa cytoskeletal protein containing a unique N-terminal region and a
C-terminal region that contains two Ig-like domains homologous
to the Ig-like domains 7 and 8 of titin <ref name="PMID:11699871">Telethonin and other new proteins of the Z-disc of skeletal muscle.</ref>.

'''Uniprot''' Q9UBF9
[http://www.uniprot.org/uniprot/Q9UBF9]

<Structure load='2KDG' size='300' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='300' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'>

'''References'''
<references />

Group:MUZIC:Myotilin

2011-06-23T15:57:47Z

Denisa Mullerova:

'''
== Myotilin ==
'''

Myotilin is a 57 kDa cytoskeletal protein containing a unique N-terminal region and a
C-terminal region that contains two Ig-like domains homologous
to the Ig-like domains 7 and 8 of titin <ref name="name for reference">Use a closing tag</ref>.

'''Uniprot''' Q9UBF9
[http://www.uniprot.org/uniprot/Q9UBF9]

<Structure load='2KDG' size='300' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='300' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'>

Group:MUZIC:Myotilin

2011-06-23T15:48:24Z

Denisa Mullerova: New page: ''' == Myotilin == ''' Myotilin is a 57 kDa cytoskeletal protein containing a unique N-terminal region and a C-terminal region that contains two Ig-like domains homologous to the Ig-like ...

'''
== Myotilin ==
'''

Myotilin is a 57 kDa cytoskeletal protein containing a unique N-terminal region and a
C-terminal region that contains two Ig-like domains homologous
to the Ig-like domains 7 and 8 of titin.

'''Uniprot''' Q9UBF9
[http://www.uniprot.org/uniprot/Q9UBF9]

<Structure load='2KDG' size='300' frame='true' align='right' caption='Solution Structure of the 1st Ig domain of Myotilin' scene='User:Denisa_Mullerova/workbench/2kdg/1'/>

<Structure load='2KKQ' size='300' frame='true' align='right' caption='Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin' scene='User:Denisa_Mullerova/workbench/2kkq/1'>