Proteopedia - User contributions [en]

Group:MUZIC:Nebulin

2013-01-18T19:50:17Z

Marie-Cecile Pelissier:

==Introduction==

Nebulin (UniProt ID: P20929 [http://www.uniprot.org/uniprot/P20929]) is a very large filamentous protein (600-900 kDa) <ref>PMID 6547565</ref> tigthly associated to the thin filament of the muscle sarcomere throughout its length. Nebulin is mostly found within the sarcomeres of skeletal muscles but was also identified at a low level in cardiac muscle cells <ref>PMID 12729758</ref>. However, the sarcomeres of cardiac muscles predominantly contain a nebulin-like protein called nebulette (UniProt ID: O76041 [http://www.uniprot.org/uniprot/O76041]) which is a "short version" of nebulin (100 kDa), highly similar to its C-terminal part <ref>PMID 8581976</ref>.

==Sequence annotation==
As illustrated on the schematic view, nebulin has a highly modular structure mostly consisting in the so-called nebulin modules. Nebulin modules are short sequences of 35 residues specific of the nebulin family of proteins. They are found in nebulin and nebulette, as well as in 3 other proteins characterized by the presence of a N-terminal LIM domain (N-RAP, Lasp-1 and Lasp-2). <ref>PMID 20951588</ref>
Whereas Nebulette is a nearly integral Z-disk protein, nebulin extends further away towards the A-band. The minimal Z-disk region of nebulin has not been clearly defined yet, but it is likely to start around the module M170 up to the SH3 domain.
Nebulin always includes the SH3 domain, and the Glutamic and Serine-rich regions, but differential splicing occurring within the nebulin modules region is the origin for a large variety of isoforms found at different developmental stages, and correlated to differences in sarcomere structure and properties, notably by affecting the Z-disk width. <ref>PMID 20176113</ref>
[[Image:Neb-Net.png|Modular organisation of Nebulin and Nebulette|600px|thumb|left|]]

==Structure==
<StructureSection load='1ark' size='300' align='right' caption='NMR structure of the SH3 domain of Nebulin' scene='User:Marie-Cecile_Pelissier/Workbench/Nebulin/Overall/2'></StructureSection>

The SH3 domain is the only domain of nebulin for which a native 3D structure is available (PDB: [[1ark]]). <ref>PMID 9514727</ref>
The nebulin SH3 domain adopts the typical <scene name='User:Marie-Cecile_Pelissier/Workbench/Nebulin/Barrel/2'>fold</scene> of a SH3 domain: it consists in a β-Barrel made of 6 β-strands which are organised in 2 anti-parallel β-sheets.

Some NMR data obtained from nebulin modules in SDS have revealed the ability of the single modules to fold into a transient helix. They were proposed to undergo a folding transition upon binding to the central groove of a monomer of F-actin. <ref>PMID 8168478</ref>

==Function and interactions==
===Function===
The nebulin protein is involved in the structural integrity of the sarcomeres and is linked to many signalling pathways crucial for the maintenance of the sarcomere.
The main functions of nebulin are <ref>PMID 20940435</ref>:
* To define and regulate the length of the thin filaments of actin (molecular ruler);
* To maintain the alignment of adjacent myofibrills (linker of adjacent Z-disks);
* To regulate muscle contraction (regulator of cross-bridge cycles).

=== Binding partners of the nebulin modules ===
*Tropomodulin: The N-terminal modules bind tropomodulin at the pointed end of the actin filament.
*Actin: Each nebulin module is able to bind to a monomer of F-actin. Even though the mechanism has not been clearly described yet, this interaction is thought to control the length of the thin filament.
*Tropomyosin/Troponin: The central super-repeats of 7 Neb modules bind 1 tropomyosin/troponin complex.
*Myosin: The central super-repeats were also shown to bind myosin in a way that would regulate the actomyosin activity.
*Calmodulin: The N-terminal and C-terminal super-repeats can bind calmodulin in a Calcium-independant manner.
*CapZ: The C-terminal modules can bind the barbed end capping protein CapZ.
*Desmin: The C-terminal modules located close to the Z-disk bind desmin, which is likely to play a role in the alignment of adjacent myofibrils.
*Alpha-Actinin: The C-terminal modules located within the Z-disk bind α-actinin

=== Binding partners of the Serine-rich region ===
The Ser-rich region has no homology to known structural motifs. The Serine residues can be phosphorylated by GSK3-β in a way that modulates some of the Nebulin interactions. <ref>PMID 21148390</ref>

=== Binding partners of the SH3 domain ===
The SH3 domain of nebulin usually interacts with the Proline-rich motif of its binding partners.
*Titin: Even though they are unlikely to be colocalised in vivo, the SH3 domain of nebulin has been proposed to bind to Pro-rich motifs located within the elastic PEVK region of titin. This has been shown in vitro. <ref name="Ma">PMID 12482578</ref>
*Myopalladin: The SH3 domain also binds the central region of myopalladin, which allows its targeting to the Z-disk.<ref>PMID 11309420</ref> <ref name="Ma">PMID 12482578</ref>
*N-WASP: The SH3 domain binds the N-WASP protein during early stages of myofibrillogenesis, this interaction promoting nucleation of the thin filament of actin. <ref>PMID 21148390</ref>

==Pathology==
Mutations in the nebulin encoding gene (NEB) are the most common cause of Nemaline myopathy (NM), a non-dystrophic congenital muscle disorder characterised by muscle weakness and hypotonia. At the cell level, the muscle fibers of patients contain rod-like “nemaline” bodies, composed of Z-disc and thin filament proteins. <ref>PMID 10051637</ref>
Mutations are of different types, deletion, missenses, frameshifts, and have been found all along the sequence of nebulin and the disease phenotypes are rather similar whatever the type or location of the mutations. The mechanism of pathogenesis is not clear yet, but it has been proposed to be linked to the loss of nebulin isoforms, because of early truncation or loss of splicing sites, the subsequent l
oss of fiber-type diversities necessary for proper muscle development. <ref>PMID 12207938</ref>

==References==

<references/><nowiki>

Group:MUZIC:Nebulin

2013-01-18T19:47:57Z

Marie-Cecile Pelissier:

==Introduction==

Nebulin (UniProt ID: P20929 [http://www.uniprot.org/uniprot/P20929]) is a very large filamentous protein (600-900 kDa) <ref>PMID 6547565</ref> tigthly associated to the thin filament of the muscle sarcomere throughout its length. Nebulin is mostly found within the sarcomeres of skeletal muscles but was also identified at a low level in cardiac muscle cells <ref>PMID 12729758</ref>. However, the sarcomeres of cardiac muscles predominantly contain a nebulin-like protein called nebulette (UniProt ID: O76041 [http://www.uniprot.org/uniprot/O76041]) which is a "short version" of nebulin (100 kDa), highly similar to its C-terminal part <ref>PMID 8581976</ref>.

==Sequence annotation==
As illustrated on the schematic view, nebulin has a highly modular structure mostly consisting in the so-called nebulin modules. Nebulin modules are short sequences of 35 residues specific of the nebulin family of proteins. They are found in nebulin and nebulette, as well as in 3 other proteins characterized by the presence of a N-terminal LIM domain (N-RAP, Lasp-1 and Lasp-2). <ref>PMID 20951588</ref>
Whereas Nebulette is a nearly integral Z-disk protein, nebulin extends further away towards the A-band. The minimal Z-disk region of nebulin has not been clearly defined yet, but it is likely to start around the module M170 up to the SH3 domain.
Nebulin always includes the SH3 domain, and the Glutamic and Serine-rich regions, but differential splicing occurring within the nebulin modules region is the origin for a large variety of isoforms found at different developmental stages, and correlated to differences in sarcomere structure and properties, notably by affecting the Z-disk width. <ref>PMID 20176113</ref>
[[Image:Neb-Net.png|Modular organisation of Nebulin and Nebulette|600px|thumb|left|]]

==Structure==
<StructureSection load='1ark' size='300' side='right' caption='NMR structure of the SH3 domain of Nebulin' scene='User:Marie-Cecile_Pelissier/Workbench/Nebulin/Overall/2'></StructureSection>

The SH3 domain is the only domain of nebulin for which a native 3D structure is available (PDB: [[1ark]]). <ref>PMID 9514727</ref>
The nebulin SH3 domain adopts the typical <scene name='User:Marie-Cecile_Pelissier/Workbench/Nebulin/Barrel/2'>fold</scene> of a SH3 domain: it consists in a β-Barrel made of 6 β-strands which are organised in 2 anti-parallel β-sheets.

Some NMR data obtained from nebulin modules in SDS have revealed the ability of the single modules to fold into a transient helix. They were proposed to undergo a folding transition upon binding to the central groove of a monomer of F-actin. <ref>PMID 8168478</ref>

==Function and interactions==
===Function===
The nebulin protein is involved in the structural integrity of the sarcomeres and is linked to many signalling pathways crucial for the maintenance of the sarcomere.
The main functions of nebulin are <ref>PMID 20940435</ref>:
* To define and regulate the length of the thin filaments of actin (molecular ruler);
* To maintain the alignment of adjacent myofibrills (linker of adjacent Z-disks);
* To regulate muscle contraction (regulator of cross-bridge cycles).

=== Binding partners of the nebulin modules ===
*Tropomodulin: The N-terminal modules bind tropomodulin at the pointed end of the actin filament.
*Actin: Each nebulin module is able to bind to a monomer of F-actin. Even though the mechanism has not been clearly described yet, this interaction is thought to control the length of the thin filament.
*Tropomyosin/Troponin: The central super-repeats of 7 Neb modules bind 1 tropomyosin/troponin complex.
*Myosin: The central super-repeats were also shown to bind myosin in a way that would regulate the actomyosin activity.
*Calmodulin: The N-terminal and C-terminal super-repeats can bind calmodulin in a Calcium-independant manner.
*CapZ: The C-terminal modules can bind the barbed end capping protein CapZ.
*Desmin: The C-terminal modules located close to the Z-disk bind desmin, which is likely to play a role in the alignment of adjacent myofibrils.
*Alpha-Actinin: The C-terminal modules located within the Z-disk bind α-actinin

=== Binding partners of the Serine-rich region ===
The Ser-rich region has no homology to known structural motifs. The Serine residues can be phosphorylated by GSK3-β in a way that modulates some of the Nebulin interactions. <ref>PMID 21148390</ref>

=== Binding partners of the SH3 domain ===
The SH3 domain of nebulin usually interacts with the Proline-rich motif of its binding partners.
*Titin: Even though they are unlikely to be colocalised in vivo, the SH3 domain of nebulin has been proposed to bind to Pro-rich motifs located within the elastic PEVK region of titin. This has been shown in vitro. <ref name="Ma">PMID 12482578</ref>
*Myopalladin: The SH3 domain also binds the central region of myopalladin, which allows its targeting to the Z-disk.<ref>PMID 11309420</ref> <ref name="Ma">PMID 12482578</ref>
*N-WASP: The SH3 domain binds the N-WASP protein during early stages of myofibrillogenesis, this interaction promoting nucleation of the thin filament of actin. <ref>PMID 21148390</ref>

==Pathology==
Mutations in the nebulin encoding gene (NEB) are the most common cause of Nemaline myopathy (NM), a non-dystrophic congenital muscle disorder characterised by muscle weakness and hypotonia. At the cell level, the muscle fibers of patients contain rod-like “nemaline” bodies, composed of Z-disc and thin filament proteins. <ref>PMID 10051637</ref>
Mutations are of different types, deletion, missenses, frameshifts, and have been found all along the sequence of nebulin and the disease phenotypes are rather similar whatever the type or location of the mutations. The mechanism of pathogenesis is not clear yet, but it has been proposed to be linked to the loss of nebulin isoforms, because of early truncation or loss of splicing sites, the subsequent l
oss of fiber-type diversities necessary for proper muscle development. <ref>PMID 12207938</ref>

==References==

<references/><nowiki>

Group:MUZIC:Nebulin

2013-01-18T19:31:28Z

Marie-Cecile Pelissier:

==Introduction==
<StructureSection load='1ark' size='300' side='right' caption='NMR structure of the SH3 domain of Nebulin' scene='User:Marie-Cecile_Pelissier/Workbench/Nebulin/Overall/2'>
Nebulin (UniProt ID: P20929 [http://www.uniprot.org/uniprot/P20929]) is a very large filamentous protein (600-900 kDa) <ref>PMID 6547565</ref> tigthly associated to the thin filament of the muscle sarcomere throughout its length. Nebulin is mostly found within the sarcomeres of skeletal muscles but was also identified at a low level in cardiac muscle cells <ref>PMID 12729758</ref>. However, the sarcomeres of cardiac muscles predominantly contain a nebulin-like protein called nebulette (UniProt ID: O76041 [http://www.uniprot.org/uniprot/O76041]) which is a "short version" of nebulin (100 kDa), highly similar to its C-terminal part <ref>PMID 8581976</ref>.

==Sequence annotation==
As illustrated on the schematic view, nebulin has a highly modular structure mostly consisting in the so-called nebulin modules. Nebulin modules are short sequences of 35 residues specific of the nebulin family of proteins. They are found in nebulin and nebulette, as well as in 3 other proteins characterized by the presence of a N-terminal LIM domain (N-RAP, Lasp-1 and Lasp-2). <ref>PMID 20951588</ref>
Whereas Nebulette is a nearly integral Z-disk protein, nebulin extends further away towards the A-band. The minimal Z-disk region of nebulin has not been clearly defined yet, but it is likely to start around the module M170 up to the SH3 domain.
Nebulin always includes the SH3 domain, and the Glutamic and Serine-rich regions, but differential splicing occurring within the nebulin modules region is the origin for a large variety of isoforms found at different developmental stages, and correlated to differences in sarcomere structure and properties, notably by affecting the Z-disk width. <ref>PMID 20176113</ref>
[[Image:Neb-Net.png|Modular organisation of Nebulin and Nebulette|800px|]]

==Structure==
</StructureSection>
The SH3 domain is the only domain of nebulin for which a native 3D structure is available (PDB: [[1ark]]). <ref>PMID 9514727</ref>
The nebulin SH3 domain adopts the typical fold of a SH3 domain: it consists in a β-Barrel made of 6 β-strands which are organised in 2 anti-parallel β-sheets.

<scene name='User:Marie-Cecile_Pelissier/Workbench/Nebulin/Barrel/2'>fold</scene>.
Some NMR data obtained from nebulin modules in SDS have revealed the ability of the single modules to fold into a transient helix. They were proposed to undergo a folding transition upon binding to the central groove of a monomer of F-actin. <ref>PMID 8168478</ref>

==Function and interactions==
===Function===
The nebulin protein is involved in the structural integrity of the sarcomeres and is linked to many signalling pathways crucial for the maintenance of the sarcomere.
The main functions of nebulin are <ref>PMID 20940435</ref>:
* To define and regulate the length of the thin filaments of actin (molecular ruler);
* To maintain the alignment of adjacent myofibrills (linker of adjacent Z-disks);
* To regulate muscle contraction (regulator of cross-bridge cycles).

=== Binding partners of the nebulin modules ===
*Tropomodulin: The N-terminal modules bind tropomodulin at the pointed end of the actin filament.
*Actin: Each nebulin module is able to bind to a monomer of F-actin. Even though the mechanism has not been clearly described yet, this interaction is thought to control the length of the thin filament.
*Tropomyosin/Troponin: The central super-repeats of 7 Neb modules bind 1 tropomyosin/troponin complex.
*Myosin: The central super-repeats were also shown to bind myosin in a way that would regulate the actomyosin activity.
*Calmodulin: The N-terminal and C-terminal super-repeats can bind calmodulin in a Calcium-independant manner.
*CapZ: The C-terminal modules can bind the barbed end capping protein CapZ.
*Desmin: The C-terminal modules located close to the Z-disk bind desmin, which is likely to play a role in the alignment of adjacent myofibrils.
*Alpha-Actinin: The C-terminal modules located within the Z-disk bind α-actinin

=== Binding partners of the Serine-rich region ===
The Ser-rich region has no homology to known structural motifs. The Serine residues can be phosphorylated by GSK3-β in a way that modulates some of the Nebulin interactions. <ref>PMID 21148390</ref>

=== Binding partners of the SH3 domain ===
The SH3 domain of nebulin usually interacts with the Proline-rich motif of its binding partners.
*Titin: Even though they are unlikely to be colocalised in vivo, the SH3 domain of nebulin has been proposed to bind to Pro-rich motifs located within the elastic PEVK region of titin. This has been shown in vitro. <ref name="Ma">PMID 12482578</ref>
*Myopalladin: The SH3 domain also binds the central region of myopalladin, which allows its targeting to the Z-disk. <ref name="Bang" /> <ref name="Ma">PMID 12482578</ref>
*N-WASP: The SH3 domain binds the N-WASP protein during early stages of myofibrillogenesis, this interaction promoting nucleation of the thin filament of actin. <ref>PMID 21148390</ref>

==Pathology==
Mutations in the nebulin encoding gene (NEB) are the most common cause of Nemaline myopathy (NM), a non-dystrophic congenital muscle disorder characterised by muscle weakness and hypotonia. At the cell level, the muscle fibers of patients contain rod-like “nemaline” bodies, composed of Z-disc and thin filament proteins. <ref>PMID 10051637</ref>
Mutations are of different types, deletion, missenses, frameshifts, and have been found all along the sequence of nebulin and the disease phenotypes are rather similar whatever the type or location of the mutations. The mechanism of pathogenesis is not clear yet, but it has been proposed to be linked to the loss of nebulin isoforms, because of early truncation or loss of splicing sites, the subsequent l
oss of fiber-type diversities necessary for proper muscle development. <ref>PMID 12207938</ref>

==References==

<references/><nowiki>

Group:MUZIC:Myopalladin

2013-01-18T17:33:24Z

Marie-Cecile Pelissier:

==Introduction==
>Myopalladin (UniProt ID: Q86TC9 [http://www.uniprot.org/uniprot/Q86TC9]) is a 145 kDa protein specific of striated muscles that was identified in a yeast two hybrid screen where the SH3 domain of nebulin (UniProt ID: P20929 [http://www.uniprot.org/uniprot/P20929],[http://www.proteopedia.org/wiki/index.php/User:Marie-Cecile_Pelissier/Workbench/Nebulin]) was used as a bait. <ref name="Bang">PMID 11309420</ref> It belongs to the family of Actin-Associated Scaffolds, which includes myotilin, palladin, and myopalladin, all three being binding partners of α-actinin (for a review, see <ref name="Otey">PMID 16164966</ref >).

==Sequence Annotation==

[[Image:Myopalladin.png |550 px|left|thumb| Modular organisation of myopalladin]]
The myopalladin protein is encoded by the MYPN gene (NM_032578).
At the protein level, myopalladin comprises 1320 amino-acids organized into 5 domains predicted to be Immunoglobulin-like domains (Ig). These Ig domains are separated by inserted sequences (IS) for which no structural domains could be predicted. The IS3 is a region of low complexity which includes some proline-rich motifs.

==Structures ==
They are currently no structural data available for myopalladin.
The only structural data related to myopalladin are the NMR structures of Ig domain 1 (PDB code 2DM2 [[http://www.proteopedia.org/wiki/index.php/2dm2]]) and Ig domain 2 (PDB code 2DM3 [[http://www.proteopedia.org/wiki/index.php/2dm3]]) of palladin (homologous to Ig domains 3 and 4 of myopalladin, respectively).

==Function and interactions==

===Function===
Myopalladin is mostly localised at the Z disk and the I band of the sarcomere in both skeletal and cardiac muscle cells, and was also found to be present in the nucleus.
It is considered to be an important structural member of the Z/I region of the sarcomere. It is involved in the targeting and anchoring of key sarcomeric components (nebulin and nebulette) to the Z-disk and takes part to the α-actinin-based mesh of the Z-disk.
Myopalladin is also thought to be related to the Z-disk signaling through its interaction with CARP, a negative regulator of muscle growth.
===Ig domains and their binding partners===
*CARP: The N-terminal region of myopalladin, going from the N-terminus of the protein to its domain Ig2, was shown to interact with the full length CARP. <ref name="Bang" />
*α-actinin: The C-terminal region of myopalladin, going from the domain Ig3 to the C-terminus of the protein, was shown to interact with the EF-hand region of α-actinin. <ref name="Bang" />
===Inserted sequences and their binding partners===
*Nebulin/Nebulette: The IS3 comprises a Proline-rich region that has been shown to interact with the SH3 domain of nebulin and nebulette. <ref name="Bang" /> <ref name="Ma">PMID 12482578</ref>

==Pathology==

Mutations of the MYPN gene were described in patients suffering from Dilated and Hypertrophic Cardiac Myopathies (DCM and HCM). <ref name="Dubosq-Bidot">PMID 18006477</ref> <ref name="Purevjav">PMID 22286171</ref> <ref name="Meyer">PMID 22892539</ref>

Many mutations were found in the α-actinin binding region of myopalladin. They are associated with a major disorganisation of muscle cells structure and sarcomere breakdown due to Z-disk instability. These effects are likely to be triggered by the mislocalisation of myopalladin within the muscle cells . <ref name="Dubosq-Bidot" /> <ref name="Meyer" /> More recently, a mutation leading to the truncation of the myopalladin C-terminus part, including both the α-actinin and nebulin binding regions, was shown to have similar effect at the cellular level. <ref name="Purevjav" />
On the other hand, a mutation located in the CARP binding-region of myopalladin (Mypn_ Y20C) prevents translocation of myopalladin to the nucleus and is primarily associated to the altered expression of myopalladin binding partners, including CARP, α -actinin and nebulin. <ref name="Purevjav" /> Surprinsingly, the down-regulation of α -actinin and nebulin does not affect the structure of the Z-disks. The main effect of this variant is likely to be due to the down-regulation of CARP and, as a consequence, to the up-regulation of CARP-repressed genes, which leads to the hypertrophic phenotype. <ref name="Purevjav" />

==References==

<references/><nowiki>

2011-07-13T13:43:05Z

Marie-Cecile Pelissier:

Group:MUZIC:Nebulin

2011-07-13T13:14:57Z

Marie-Cecile Pelissier:

Group:MUZIC:Nebulin

2011-07-13T13:14:38Z

Marie-Cecile Pelissier:

2011-07-13T12:59:13Z

Marie-Cecile Pelissier:

Group:MUZIC:Nebulin

2011-07-13T12:58:20Z

Marie-Cecile Pelissier:

Group:MUZIC:Nebulin

2011-07-13T12:58:02Z

Marie-Cecile Pelissier:

2011-07-13T11:22:13Z

Marie-Cecile Pelissier:

Group:MUZIC:Nebulin

2011-07-13T11:21:11Z

Marie-Cecile Pelissier:

Group:MUZIC:Nebulin

2011-07-13T11:20:48Z

Marie-Cecile Pelissier:

<StructureSection load='1ark' size='500' side='right' caption='NMR structure of the SH3 domain of Nebulin' scene='User:Marie-Cecile_Pelissier/Workbench/Nebulin/Overall/2'>
==Introduction==
Nebulin (UniProt ID: P20929 [http://www.uniprot.org/uniprot/P20929]) is a very large filamentous protein (600-900 kDa) <ref>PMID 6547565</ref> tightly associated to the thin filament of the muscle sarcomere throughout its length. Nebulin is mostly found within the sarcomeres of skeletal muscles but was also identified at a low level in cardiac muscle cells <ref>PMID 12729758</ref>. However, the sarcomeres of cardiac muscles predominantly contain a Nebulin-like protein called Nebulette (UniProt ID: O76041 [http://www.uniprot.org/uniprot/O76041]) which is a "short version" of Nebulin (100 kDa), highly similar to its C-terminal part <ref>PMID 8581976</ref>.

==Function==

The Nebulin protein is involved in the structural integrity of the sarcomeres and is linked to many signalling pathways crucial for the maintenance of the sarcomere.
The main fucntions of Nebulin are <ref>PMID 20940435</ref>:
1. To define and regulate the length of the thin filaments of actin (molecular ruler);
2. To maintain the alignment of adjacent myofibrills (linker of adjacent Z-disks);
3. To regulate muscle contraction (regulator of cross-bridge cycles).

Mutations in the Nebulin encoding gene are the most common cause of Nemaline myopathy (NM), a non-dystrophic congenital muscle disorder characterised by muscle weakness.
</StructureSection>
----

== Domains and interactions==
[[Image:Neb-Net.png|Modular organisation of Nebulin and Nebulette|400px|right|thumb|]]

=== Glutamic rich region ===

=== Nebulin modules ===

=== Serine rich region ===

=== SH3 domain ===

The Nebulin SH3 domain adopts a ß-Barrel <scene name='User:Marie-Cecile_Pelissier/Workbench/Nebulin/Barrel/2'>fold</scene>.
The SH3 domain is the only domain of Nebulin for which a 3D structure is available.

==References==

<references/><nowiki>

Group:MUZIC:Myopalladin

2011-07-13T11:18:19Z

Marie-Cecile Pelissier:

Group:MUZIC:Myopalladin

2011-07-13T10:21:02Z

Marie-Cecile Pelissier:

Group:MUZIC:Myopalladin

2011-07-13T10:20:39Z

Marie-Cecile Pelissier: