ArticleJournal of muscle research and cell motility1999
The Drosophila projectin mutant, bentD, has reduced stretch activation and altered indirect flight muscle kinetics.
Article in Journal of muscle research and cell motility, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Fine-tuning striated muscle performance: conserved sarcomere-level mechanisms across insect and vertebrate systems.Frontiers in physiology · 2026Review
- Transcriptional regulation and alternative splicing cooperate in muscle fiber-type specification in flies and mammals.Experimental cell research · 2014Review
- 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
- Transcriptome and gene expression analysis of the rice leaf folder, Cnaphalocrosis medinalis.PloS one · 2012Article
- 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
- Site directed mutagenesis of Drosophila flightin disrupts phosphorylation and impairs flight muscle structure and mechanics.Journal of muscle research and cell motility · 2007Article
- Passive stiffness in Drosophila indirect flight muscle reduced by disrupting paramyosin phosphorylation, but not by embryonic myosin S2 hinge substitution.Biophysical journal · 2006Article
- The molecular elasticity of the insect flight muscle proteins projectin and kettin.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Elementary steps of the cross-bridge cycle in fast-twitch fiber types from rabbit skeletal muscles.Biophysical journal · 2005Article
- Paramyosin phosphorylation site disruption affects indirect flight muscle stiffness and power generation in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- In indirect flight muscles Drosophila projectin has a short PEVK domain, and its NH2-terminus is embedded at the Z-band.Journal of muscle research and cell motility · 2005Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Projectin is a ca. 900 kDa protein that is a member of the titin protein superfamily. In skeletal muscle titins are involved in the longitudinal reinforcement of the sarcomere by connecting the Z-band to the M-line. In insect indirect flight muscle (IFM), projectin is believed to form the connecting filaments that link the Z-band to the thick filaments and is responsible for the high relaxed stiffness found in this muscle type. The Drosophila mutant bentD (btD) has been shown to have a breakpoint close to the carboxy-terminal kinase domain of the projectin sequence. Homozygotes for btD are embryonic lethal but heterozygotes (btD/+) are viable. Here we show that btD/+ flies have normal flight ability and a slightly elevated wing beat frequency (btD/+ 223+/-13 Hz; +/+ 203+/-5 Hz, mean +/- SD; P < 0.01). Electron microscopy of btD/+ IFM show normal ultrastructure but skinned fiber mechanics show reduced stretch activation and oscillatory work. Although btD/+ IFM power output was at wild-type levels, maximum power was achieved at a higher frequency of applied length perturbation (btD/+ 151+/-6 Hz; +/+ 102+/-14 Hz; P < 0.01). Results were interpreted in the context of a viscoelastic model of the sarcomere and indicate altered cross-bridge kinetics of the power-producing step. These results show that the btD mutation reduces oscillatory work in a way consistent with the proposed role of the connecting filaments in the stretch activation response of IFM.
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