Group:MUZIC:CapZ: Difference between revisions

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== Introduction ==

CapZ is expressed in all eukaryotic cells. BLAST analysis shows high sequence conservation across mammals. It binds to the fast growing barbed ends of [[actin]] filaments and blocks G-actin association and disassociation, thus regulating actin filament dynamics. In skeletal muscle it localizes at the Z-disk. CapZ is a heterodimer composed of two subunits <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Alpha_subunit/1'>α</scene> and <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Beta_subunit/1'>β</scene> and there are at least two isoforms of each of the subunits. In cardiomyocites the β1 containing isoform localizes to the Z-disk and β2 containing isoform localizes to the cell periphery and intercalated disc.

Capping protein, also known as CapZ in muscle, is expressed in all eukaryotic cells. BLAST analysis shows high sequence conservation across mammals. It binds to the fast growing barbed ends of [[actin]] filaments and blocks G-actin association and disassociation, thus regulating actin filament dynamics. In skeletal muscle it localizes at the Z-disk. CapZ is a heterodimer composed of two subunits <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Alpha_subunit/1'>α</scene> and <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Beta_subunit/1'>β</scene> and there are at least two isoforms of each of the subunits. In cardiomyocites the β1 containing isoform localizes to the Z-disk and β2 containing isoform localizes to the cell periphery and intercalated disc.

The crystal structure of the sarcomeric form has been resolved to a resolution of 2.1 Å by X-ray crystallography (1IZN). <ref>PMID:12660160</ref>

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== Pathology ==

The absence of capping protein prevented the reconstruction of motility in Shigella and Listeria, in vitro <ref>PMID:16416311</ref>. Small interference RNA (siRNA) studies showed that knockdown of nebulin in chick skeletal myotubes leads to a reduction of assembled CapZ and a loss of the characteristic uniform alignment of the barbed ends of F-actin and this suggests that the interaction of CapZ and nebulin plays an important role in Z-disk architecture <ref>PMID:18272787</ref>.

==References==

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 == Introduction ==
-CapZ is expressed in all eukaryotic cells. BLAST analysis shows high sequence conservation across mammals. It binds to the fast growing barbed ends of [[actin]] filaments and blocks G-actin association and disassociation, thus regulating actin filament dynamics. In skeletal muscle it localizes at the Z-disk. CapZ is a heterodimer composed of two subunits <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Alpha_subunit/1'>α</scene> and <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Beta_subunit/1'>β</scene> and there are at least two isoforms of each of the subunits. In cardiomyocites the β1 containing isoform localizes to the Z-disk and β2 containing isoform localizes to the cell periphery and intercalated disc.
+Capping protein, also known as CapZ in muscle, is expressed in all eukaryotic cells. BLAST analysis shows high sequence conservation across mammals.  It binds to the fast growing barbed ends of [[actin]] filaments and blocks G-actin association and disassociation, thus regulating actin filament dynamics. In skeletal muscle it localizes at the Z-disk. CapZ is a heterodimer composed of two subunits <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Alpha_subunit/1'>α</scene> and <scene name='User:Mara_Camelia_Rusu/Workbench/CapZ/Beta_subunit/1'>β</scene> and there are at least two isoforms of each of the subunits. In cardiomyocites the β1 containing isoform localizes to the Z-disk and β2 containing isoform localizes to the cell periphery and intercalated disc.
 The crystal structure of the sarcomeric form has been resolved to a resolution of 2.1 Å by X-ray crystallography (1IZN). <ref>PMID:12660160</ref>
 <Structure load='1IZN' size='500' frame='true' align='right' caption='Crystal structure of chicken CapZ expressed in E.coli' scene='Insert optional scene name here' />
@@ Line 24: / Line 24: @@
 == Pathology ==
 The absence of capping protein prevented the reconstruction of motility in Shigella and Listeria, in vitro <ref>PMID:16416311</ref>. Small interference RNA (siRNA) studies showed that knockdown of nebulin in chick skeletal myotubes leads to a reduction of assembled CapZ and a loss of the characteristic uniform alignment of the barbed ends of F-actin and this suggests that the interaction of CapZ and nebulin plays an important role in Z-disk architecture <ref>PMID:18272787</ref>.
 ==References==