Titin, a huge, elastic sarcomeric protein with a probable role in morphogenesis

@article{Fulton1991TitinAH,
  title={Titin, a huge, elastic sarcomeric protein with a probable role in morphogenesis},
  author={Alice Bordwell Fulton and William B. Isaacs},
  journal={BioEssays},
  year={1991},
  volume={13}
}
Titin, the largest protein identified to date (over 1 μm long, almost 3 million daltons in mass) is the third most abundant component of the sarcomere. In the mature myofibril, titin molecules span from M line to Z line, forming a third filament system which provides sarcomeric alignment and elastic recoil. In the developing sarcomere, accumulating evidence from studies both in vivo and in vitro implicates titin as part of a morphogenetic scaffolding, upon which critical events in… Expand
Immunoglobulin-type domains of titin: same fold, different stability?
TLDR
The stability of the modules over a range of conditions was investigated by measuring key thermodynamic parameters for both thermal and chemical denaturation and by monitoring amide proton exchange as a function of time. Expand
Structure and function of titin and nebulin.
  • T. Keller
  • Biology, Medicine
  • Current opinion in cell biology
  • 1995
TLDR
The characterization of a cellular (non-muscle) isoform of titin has extended the functional relevance of this family of proteins beyond the realm of muscle. Expand
Titin role in muscle homeostasis : the kinase domain
TLDR
It was demonstrated that TK is a catalytically inactive pseudokinase acting as a molecular scaffold and TK and MuRF1 signaling modules are structurally interconnected and genetic perturbation of this link might lead to dilated cardiomyopathy. Expand
The anatomy of a molecular giant: how the sarcomere cytoskeleton is assembled from immunoglobulin superfamily molecules.
Cross-striated muscle contains an elastic cytoskeleton comprised of the giant protein titin and several associated proteins. cDNA sequencing revealed that all these proteins are immunoglobulinExpand
Biochemical and Structural Properties of Titin , Nebulin and Intermediate Filaments in Muscle
TLDR
The Z-line is a key structure of the myofibrils and of the overall skeletal muscle cell cytoskeleton and can be considered as “representing,” or taking the place of, the microfilaments of non-muscle cells. Expand
Dissecting titin into its structural motifs: identification of an alpha-helix motif near the titin N-terminus.
TLDR
A study of a stretch located in the titin N-terminus and part of a linker between two modules is presented, drawn toward this region because it shows 100% probability to form a coiled coil when analyzed by a prediction program. Expand
Titin and Nebulin: Giant Multitasking Protein Rulers in Muscle
When a striated muscle cell is stimulated, e.g. by nerve impulses, it is activated from the resting state. It develops contractile force, shortens, and then relengthens to its original dimension whenExpand
The genetics and molecular biology of the titin/connectin-like proteins of invertebrates.
TLDR
A substantial amount of information has been gathered about the structure and function of twitchin/titin-related proteins in the invertebrates through sequence analysis and the analysis of loss-offunction phenotypes, but a number of fascinating questions remain. Expand
Smitin, a novel smooth muscle titin–like protein, interacts with myosin filaments in vivo and in vitro
TLDR
It is found that avian vascular and visceral smooth muscles contain a novel, megadalton protein, smitin, that is similar to striated muscle titin in molecular morphology, localization in a contractile apparatus, and ability to interact with myosin filaments. Expand
Thick filament assembly occurs after the formation of a cytoskeletal scaffold
TLDR
It is concluded that the correct assembly of a cytoskeletal scaffold is a prerequisite for correct thick filament assembly and for the integration of the contractile apparatus into the myofibril. Expand
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References

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Titin is an extraordinarily long, flexible, and slender myofibrillar protein.
TLDR
Electron microscopy of low-angle-shadowed and negatively stained specimens revealed that T2 chains self-assembled into extremely long, flexible, and extensible slender strands with axial periodicity, suggesting titin appears to be ideally suited as a component of an elastic lattice that serves as an organizing scaffold or template for thick and thin filaments. Expand
Does titin regulate the length of muscle thick filaments?
TLDR
The protein titin has been localized by electron microscopy of myofibrils labelled with monoclonal antibodies, and molecules of titin in this configuration provided an obvious mechanism by which the length of thick filaments could be regulated accurately. Expand
Cytoskeletal matrix in striated muscle: the role of titin, nebulin and intermediate filaments.
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TLDR
The recognition of the existence of two sets of sarcomere-associated cytoskeletal filaments within adult striated muscle fibers may be a significant step toward resolving some of the unsettled questions in muscle mechanics such as those that have been discussed in this meeting. Expand
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TLDR
The ability of single skinned muscle cells to generate both passive tension in response to stretch and active tension in Response to calcium is greatly reduced after low doses of ionizing radiation, accompanied by axial misalignment of thick filaments. Expand
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TLDR
Observations suggest that newly synthesized titin molecules are stable proteins that rapidly associate with the cytoskeleton of developing myotubes. Expand
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The sarcomere, the basic contractile unit of striated muscle cells, is widely accepted as being constructed of two sets of parallel and interdigitated protein filaments that are discontinuous andExpand
A regular pattern of two types of 100-residue motif in the sequence of titin
TLDR
It is shown that partial titin complementary DNAs encode a regular pattern of two types of 100-residue motif, each of which probably folds into a separate domain type. Expand
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TLDR
A wide range of phyla have been surveyed by SDS-PAGE for the new large proteins of the myofibril, and Connectin (or titin) appears to be widely distributed and nebulin shares the same distribution in vertebrate muscles except for its notable absence in all heart muscle examined. Expand
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TLDR
Studies of electrophoretic mobility on 2-3% polyacrylamide gel electrophoresis, amino acid composition, and localization in myofibrils determined by the indirect immunofluorescence technique showed that titin and connectin are identical. Expand
Titin: Quantitative mass measurements by scanning transmission electron microscopy and structural implications for the sarcomere matrix of skeletal muscle
TLDR
A single native intact titin molecule has a calculated contour length of well above ∼1 μm, sufficient to span unidirectionally between the Z line and M line region in a resting‐length sarcomere. Expand
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