Modular proteins from the Drosophila sallimus (sls) gene and their expression in muscles with different extensibility.

@article{Burkart2007ModularPF,
  title={Modular proteins from the Drosophila sallimus (sls) gene and their expression in muscles with different extensibility.},
  author={C. Burkart and Feng Qiu and S. Brendel and V. Bene{\vs} and P. H{\aa}{\aa}g and S. Labeit and K. Leonard and B. Bullard},
  journal={Journal of molecular biology},
  year={2007},
  volume={367 4},
  pages={
          953-69
        }
}
The passive elasticity of the sarcomere in striated muscle is determined by large modular proteins, such as titin in vertebrates. In insects, the function of titin is divided between two shorter proteins, projectin and sallimus (Sls), which are the products of different genes. The Drosophila sallimus (sls) gene codes for a protein of 2 MDa. The N-terminal half of the protein is largely made up of immunoglobulin (Ig) domains and unique sequence; the C-terminal half has two stretches of sequence… Expand
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TLDR
In immuno-localization was used to show that the N-termini of projectin and Salimus are inserted into the Z-band, and structural information may help provide an interpretive framework for future studies using this muscle system. Expand
Elastic proteins in the flight muscle of Manduca sexta.
TLDR
Analysis of the gene sequence showed that all 4 putative Sallimus and kettin isoforms could be explained as products of alternative splicing of the single sls gene, and both projectin and sallimus isoforms were expressed to higher levels in ventrally located DLM1 subunits, primarily responsible for active work production, as compared to dorsally located subunits which may act as damped springs. Expand
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Sallimus and the dynamics of sarcomere assembly in Drosophila flight muscles.
TLDR
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TLDR
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It is concluded that obscurin in the IFM is necessary for the development of a symmetrical sarcomere in Drosophila IFM. Expand
Huxleys' Missing Filament: Form and Function of Titin in Vertebrate Striated Muscle.
TLDR
Although superthin filaments were inferred from early experiments on muscle, decades passed before their existence was accepted, recent studies demonstrate unequivocally that titin stiffness increases upon muscle activation, but the mechanisms are only now being uncovered. Expand
Binding partners of the kinase domains in Drosophila obscurin and their effect on the structure of the flight muscle
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Titin and Nebulin in Thick and Thin Filament Length Regulation.
TLDR
The history and the current state of ideas related to the mechanism of size regulation of the thick and thin filaments in vertebrate striated muscles are discussed, with evidence pointing to titin and nebulin stabilizing structures of the respective filaments. Expand
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Some Functions of Proteins from the Drosophila sallimus (sls) Gene
Insect flight muscles contract at high frequencies and are activated by periodically stretching the muscles. For the stretch to have an effect, the muscles must be stiff. Two elastic proteins,Expand
Varieties of elastic protein in invertebrate muscles.
TLDR
The wormlike chain model for polymer elasticity fitted the force-extension curve of IFM myofibrils and the number of predicted IGS in the chain is consistent with the tandem Igs in Drosophila SLS protein, concluding that passive tension is due to kettin and projectin. Expand
Section: Elastic Invertebrate Muscle Proteins; Varieties of elastic protein in invertebrate muscles
TLDR
The wormlike chain model for polymer elasticity fitted the force-extension curve of IFM myofibrils and the number of predicted IGS in the chain is consistent with the tandem Igs in Drosophila SLS protein, concluding that passive tension is due to kettin and projectin. Expand
Sequence and expression of the kettin gene in Drosophila melanogaster and Caenorhabditis elegans.
TLDR
The sequence of a 21.3 kb contig of the Drosophila kettin gene has been determined and the structure of the flight muscle in all the heterozygous mutants was normal, including the myofibril-cuticle connections, and they were able to fly. Expand
Alternative splicing of an amino-terminal PEVK-like region generates multiple isoforms of Drosophila projectin.
TLDR
The completion of the projectin sequence analysis is described, which defines projectin as a 1 MDa protein, composed of 39 immunoglobulin and 39 fibronectin III domains, and leads to the identification of a domain rich in the amino acids P, E, V and K within the NH(2) terminus of projectin. Expand
Stretchin-klp, a novel Drosophila indirect flight muscle protein, has both myosin dependent and independent isoforms
TLDR
These studies suggest that this newly identified stretchin-klp protein is a major component of the Drosophila IFM thick filament. Expand
The function of elastic proteins in the oscillatory contraction of insect flight muscle
TLDR
Insect flight muscle has multiple elastic proteins to give the sarcomere the optimum compliance necessary for high frequency oscillatory contraction. Expand
Drosophila stretchin-MLCK is a novel member of the Titin/Myosin light chain kinase family.
Members of the titin/myosin light chain kinase family play an essential role in the organization of the actin/myosin cytoskeleton, especially in sarcomere assembly and function. In DrosophilaExpand
Kettin, a large modular protein in the Z‐disc of insect muscles.
TLDR
It is suggested that the protein acts as scaffolding in the Z‐disc and is called kettin, which may cause disintegration of the Z-disc and alpha‐actinin release which lead to disassembly of the myofibril. Expand
Structurally differentDrosophila striated muscles utilize distinct variants of Z-band-associated proteins
TLDR
Despite their different locations, the projectins of synchronous and asynchronous muscles are very similar, but not identical, as judged by SDS-PAGE and by peptide mapping. Expand
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