Group:MUZIC: Difference between revisions

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Thin filaments (actin) from adjacent sarcomeres are anchored at the Z-disc. In this area of the sarcomere, each actin filament overlaps with four filaments from the opposite sarcomere, forming a square lattice, which is cross-connected in a zig-zag pattern by α-actinin-2 <ref>PMID:19830582</ref> (Figure 2). This region plays a central role as the main anchoring point of the molecular machinery for muscle contraction comprising the actin, titin, and nebulin filaments <ref>PMID:22028589</ref><ref>PMID:9476658</ref>.

Z-discs are also implicated in mechanosensing and signaling to the nucleus, which contribute to maintenance of muscle homeostasis, and serve as attachment sites for desmin intermediate filaments and often for transverse tubules [reviewed in <ref>PMID:12556452</ref><ref>PMID:21190822</ref><ref>PMID:21347754</ref>]. The assembly of the Z-disc is controlled via N-terminal part of titin, which exhibits binding sites for α-actinin-2 as well as to additional Z-disc components. The most striking feature of muscle and Z-disc proteins, in particular, is the diversity of multiple protein-protein interactions that form part of a complex network, involving more than forty proteins<ref name="r2">PMID:12142273</ref><ref>PMID:16416311</ref><ref>PMID:15810059</ref> (Figure 3). For example, titin binds to α-actinin-2 via 45-residue sequence motifs, the so-called Z-repeats <ref>PMID:9003807</ref> and dimerizes at its N-terminal through the mediator protein telethonin <ref>PMID:16407954</ref>.

~~==About MUZIC==~~

The MUZIC network provides a unique mix of cellular and structural biology laboratories with a focus on muscle research and combines a series of complementary state-of-the art know-how and technologies ranging from high resolution (X-ray crystallography) and low resolution structural biology methods (SAXS, EM, cryo-EM tomography, atomic force microscopy) to a variety of cell biology oriented techniques, ranging from FRET and live-cell imaging, cellular and animal models to animal physiology. These are complemented by a biochemical and biophysical characterisation of proteins and their complexes.

==References==

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    Thin filaments (actin) from adjacent sarcomeres are anchored at the Z-disc. In this area of the sarcomere, each actin filament overlaps with four filaments from the opposite sarcomere, forming a square lattice, which is cross-connected in a zig-zag pattern by α-actinin-2 <ref>PMID:19830582</ref> (Figure 2). This region plays a central role as the main anchoring point of the molecular machinery for muscle contraction comprising the actin, titin, and nebulin filaments <ref>PMID:22028589</ref><ref>PMID:9476658</ref>.
    Z-discs are also implicated in mechanosensing and signaling to the nucleus, which contribute to maintenance of muscle homeostasis, and serve as attachment sites for desmin intermediate filaments and often for transverse tubules [reviewed in <ref>PMID:12556452</ref><ref>PMID:21190822</ref><ref>PMID:21347754</ref>]. The assembly of the Z-disc is controlled via N-terminal part of titin, which exhibits binding sites for α-actinin-2 as well as to additional Z-disc components. The most striking feature of muscle and Z-disc proteins, in particular, is the diversity of multiple protein-protein interactions that form part of a complex network, involving more than forty proteins<ref name="r2">PMID:12142273</ref><ref>PMID:16416311</ref><ref>PMID:15810059</ref> (Figure 3). For example, titin binds to α-actinin-2 via 45-residue sequence motifs, the so-called Z-repeats <ref>PMID:9003807</ref> and dimerizes at its N-terminal through the mediator protein telethonin <ref>PMID:16407954</ref>.
-==About MUZIC==
-The MUZIC network provides a unique mix of cellular and structural biology laboratories with a focus on muscle research and combines a series of complementary state-of-the art know-how and technologies ranging from high resolution (X-ray crystallography) and low resolution structural biology methods (SAXS, EM, cryo-EM tomography, atomic force microscopy) to a variety of cell biology oriented techniques, ranging from FRET and live-cell imaging, cellular and animal models to animal physiology. These are complemented by a biochemical and biophysical characterisation of proteins and their complexes.
 ==References==
 <references/>