Drosophila D-titin is required for myoblast fusion and skeletal muscle striation
| Autor: | Emma Rushton, Warren S. Davis, Yong Zhang, David E. Featherstone, Kendal Broadie |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Myofilament
animal structures Molecular Sequence Data Muscle Proteins Genes Insect macromolecular substances Cell Fusion P element Myoblast fusion Myofibrils medicine Animals Drosophila Proteins Connectin Muscle Skeletal Genetics Base Sequence biology Myogenesis Alternative splicing Chromosome Mapping Skeletal muscle Cell Biology musculoskeletal system biology.organism_classification Protein Structure Tertiary Actin Cytoskeleton Mutagenesis Insertional Drosophila melanogaster medicine.anatomical_structure Ethyl Methanesulfonate biology.protein Insect Proteins Genes Lethal Titin Protein Kinases tissues Mutagens |
| Zdroj: | Journal of Cell Science. 113:3103-3115 |
| ISSN: | 1477-9137 0021-9533 |
| DOI: | 10.1242/jcs.113.17.3103 |
| Popis: | An ethylmethane sulfonate (EMS) mutagenesis of Drosophila melanogaster aimed at discovering novel genes essential for neuromuscular development identified six embryonic lethal alleles of one genetic locus on the third chromosome at 62C. Two additional lethal P element insertion lines, l(3)S02001 and l(3)j1D7, failed to complement each other and each of the six EMS alleles. Analysis of genomic sequence bracketing the two insertion sites predicted a protein of 16,215 amino acid residues, encoded by a 70 kb genomic region. This sequence includes the recently characterized kettin, and includes all known partial D-Titin sequences. We call the genetic locus, which encodes both D-Titin and kettin, D-Titin. D-Titin has 53 repeats of the immunoglobulin C2 domain, 6 repeats of the fibronectin type III domain and two large PEVK domains. Kettin appears to be the NH2-terminal one third of D-Titin, presumably expressed via alternative splicing. Phenotype assays on the allelic series of D-Titin mutants demonstrated that D-Titin plays an essential role in muscle development. First, D-Titin has an unsuspected function in myoblast fusion during myogenesis and, second, D-Titin later serves to organize myofilaments into the highly ordered arrays underlying skeletal muscle striation. We propose that D-Titin is instrumental in the development of the two defining features of striated muscle: the formation of multi-nucleate syncitia and the organization of actin-myosin filaments into striated arrays. |
| Databáze: | OpenAIRE |
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