ArticleJournal of muscle research and cell motility2005
In indirect flight muscles Drosophila projectin has a short PEVK domain, and its NH2-terminus is embedded at the Z-band.
Article in Journal of muscle research and cell motility, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Fine-tuning striated muscle performance: conserved sarcomere-level mechanisms across insect and vertebrate systems.Frontiers in physiology · 2026Review
- Article
- Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes.The Journal of cell biology · 2020Article
- Elastic proteins in the flight muscle of Manduca sexta.Archives of biochemistry and biophysics · 2015Article
- Molecular analysis of the muscle protein projectin in Lepidoptera.Journal of insect science (Online) · 2013Article
- Genetic elevation of sphingosine 1-phosphate suppresses dystrophic muscle phenotypes in Drosophila.Development (Cambridge, England) · 2013Article
- The myofibrillar protein, projectin, is highly conserved across insect evolution except for its PEVK domain.Journal of molecular evolution · 2008Article
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Insect indirect flight muscles (IFM) contain a third filament system made up of elastic connecting or C-filaments. The giant protein projectin is the main, if not the only, component of these structures. In this study we found that projectin is oriented within the IFM sarcomere with its NH2-terminus embedded in the Z-bands. We demonstrate that this protein has an elastic region that can be detected by the movement of specific epitopes following stretch. One possible elastic region is the PEVK-like domain located close to the NH2-terminus. The amino acid length of this region is short, and 52% of its residues are P, E, V or K. We propose a model in which projectin extends from the Z-band to the lateral borders of the A-band. The PEVK-like domain and a series of Ig domains spanning the intervening I-band may provide the elastic properties of projectin.
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