Two immunoglobulin‐like domains of the Z‐disc portion of titin interact in a conformation‐dependent way with telethonin

@article{Mues1998TwoID,
  title={Two immunoglobulin‐like domains of the Z‐disc portion of titin interact in a conformation‐dependent way with telethonin},
  author={Alexander Mues and Peter F.M. van der Ven and Paul Young and Dieter O. F{\"u}rst and Mathias Gautel},
  journal={FEBS Letters},
  year={1998},
  volume={428}
}
The giant protein titin. Emerging roles in physiology and pathophysiology.
Titin is a giant protein of vertebrate striated muscles (M(r), > or = 3000 kD). Its molecules are of filamentous shape and span from the Z disk to the M line, thereby forming a third filament system
Fishing out proteins that bind to titin
TLDR
Another giant protein has been detected in cross-striated muscle cells, and it was discovered in a yeast two-hybrid screen in which the bait was a small region of titin that is localized near the Z-band.
Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly
TLDR
The presence of a calmodulin-binding IQ motif, and a Rho guanine nucleotide exchange factor domain in the COOH-terminal region suggest that obscurin is involved in Ca2+/calmodulin, as well as G protein–coupled signal transduction in the sarcomere.
Dynamic Strength of Titin's Z-Disk End
TLDR
Experimental results on the dynamic strength of titin's Z1Z2 domains measured by nanomechanical manipulation of the chemical dimer of a recombinant protein fragment are reported.
Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1
TLDR
The dual interactions of MURF-1 with titin and GMEB-1 may link myofibril signaling pathways (perhaps including titin's kinase domain) with muscle gene expression, suggesting the stability of the sarcomeric M-line region.
Functional properties of the titin/connectin-associated proteins, the muscle-specific RING finger proteins (MURFs), in striated muscle
TLDR
How they may tie together titin-mediated myofibril signaling pathways (perhaps involving the titin kinase domain), biomechanical signaling, the muscle stress response, and gene expression is discussed.
Titin‐cap associates with, and regulates secretion of, Myostatin
TLDR
T‐cap, by interacting with Myostatin, controls Myostati secretion in myogenic precursor cells without affecting the processing step of precursor MyostAT, according to a yeast two‐hybrid screen.
Structural basis for activation of the titin kinase domain during myofibrillogenesis
TLDR
The crystal structure of titin's only catalytic domain is presented, an autoregulated serine kinase (titin kinase), and the structure shows how the active site is inhibited by a tyrosine of the kinase domain.
Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk
TLDR
This work shows, using X-ray crystallography, how the amino terminus of the longest filament component, the giant muscle protein titin, is assembled into an antiparallel (2:1) sandwich complex by the Z-disk ligand telethonin.
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References

SHOWING 1-10 OF 21 REFERENCES
The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers.
TLDR
A serine/proline rich site, which can be phosphorylated by kinases in developing muscle tissues, was identified near the amino terminus of titin and sequence analysis revealed the presence of a novel 45 residue repeat ('Z-repeats') in this region of the molecule.
The N-Terminal Z Repeat 5 of Connectin/Titin Binds to the C-Terminal Region of α-Actinin
TLDR
Using the yeast two-hybrid system, the present work shows that the N-terminal Z repeat 5 region of connectin binds to the C-Terminal region of α-actinin, the main constituent of the Z line.
Molecular structure of the sarcomeric Z‐disk: two types of titin interactions lead to an asymmetrical sorting of α‐actinin
TLDR
A molecular model of the sarcomeric Z‐disk, where overlapping titin filaments and their interactions with the α‐actinin rod and C‐terminal domain can account for the essential ultrastructural features is proposed.
A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy.
TLDR
The interaction of recombinant titin with overlapping fragments of human cardiac MyBP-C maps the titin-binding site within the C-terminal region, which is deleted in patients suffering from the chromosome-11-associated form of familial hypertrophic cardiomyopathy, likely to be the result of thick-filament misassembly by abolishing the ternary interaction of titin, myosin and My BP-C.
Titins: Giant Proteins in Charge of Muscle Ultrastructure and Elasticity
TLDR
The architecture of sequences in the A band region of titin suggests why thick filament structure is conserved among vertebrates and compares two elements that correlate with tissue stiffness that suggest that titin may act as two springs in series.
Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin
TLDR
It is proposed that this demonstration of a phosphorylation‐controlled interaction in the sarcomeric cytoskeleton is of potential relevance for sarcomere formation and/or turnover and also reveals how binding affinities of modular proteins can be regulated by modifications of inter‐domain linkers.
Titin aggregates associated with intermediate filaments align along stress fiber-like structures during human skeletal muscle cell differentiation.
TLDR
It is concluded that IF and SFLS play an important role in the very early stages of in vitro human myofibrillogenesis and the association of titin with SFLs might be crucial for the unwinding of titan necessary for the assembly of sarcomeres and the first association of Titin with other sarcomeric proteins.
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