ArticleBiochemical genetics1994
Alterations in flightin phosphorylation in Drosophila flight muscles are associated with myofibrillar defects engendered by actin and myosin heavy-chain mutant alleles.
Article in Biochemical genetics, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Molecular Characterization and Phylogenetic Analysis of Flightin Gene inAnimals : an open access journal from MDPI · 2024Article
- Review
- An evolutionary analysis of flightin reveals a conserved motif unique and widespread in Pancrustacea.Journal of molecular evolution · 2014Article
- COOH-terminal truncation of flightin decreases myofilament lattice organization, cross-bridge binding, and power output in Drosophila indirect flight muscle.American journal of physiology. Cell physiology · 2011Article
- Alternative S2 hinge regions of the myosin rod differentially affect muscle function, myofibril dimensions and myosin tail length.Journal of molecular biology · 2007Article
- 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
- Stretchin-klp, a novel Drosophila indirect flight muscle protein, has both myosin dependent and independent isoforms.Journal of muscle research and cell motility · 2005Article
- Overexpression of miniparamyosin causes muscle dysfunction and age-dependant myofibril degeneration in the indirect flight muscles of Drosophila melanogaster.Journal of muscle research and cell motility · 2001Article
- Flightin is essential for thick filament assembly and sarcomere stability in Drosophila flight muscles.The Journal of cell biology · 2000Article
- Flight muscle function in Drosophila requires colocalization of glycolytic enzymes.Molecular biology of the cell · 1997Article
Corrections and comments
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1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flightin is a 20-kD myofibrillar protein found in the stretch-activated flight muscles of Drosophila melanogaster. Nine of the eleven isoelectric variants of flightin are generated in vivo by multiple phosphorylations. The accumulation of these isoelectric variants is affected differently by mutations that eliminate thick filaments or thin filaments. Mutations in the myosin heavy-chain gene that prevent thick filament assembly block accumulation of all flightin variants except N1, the unphosphorylated precursor, which is present at much reduced levels. Mutations in the flight muscle-specific actin gene that block actin synthesis and prevent thin filament assembly disrupt the temporal regulation of flightin phosphorylation, resulting in premature phosphorylation and premature accumulation of flightin phosphovariants. Cellular fractionation of fibers that are devoid of thin filaments show that flightin remains associated with the thick filament-rich cytomatrix. These results suggest that flightin is a structural component of the thick filaments whose regulated phosphorylation is dependent upon the presence of thin filaments.
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