ArticleThe Journal of cell biology2000
Flightin is essential for thick filament assembly and sarcomere stability in Drosophila flight muscles.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 107 citations in OpenAlex.
- Insufficient wing development possibly contributes to flightlessness of the silkwormProceedings. Biological sciences · 2025Article
- Two Forms of Thick Filament in the Flight Muscle ofInternational journal of molecular sciences · 2024Article
- Immune system modulation & virus transmission during parasitism identified by multi-species transcriptomics of a declining insect biocontrol system.BMC genomics · 2024Article
- Molecular Characterization and Phylogenetic Analysis of Flightin Gene inAnimals : an open access journal from MDPI · 2024Article
- Knockdown ofFrontiers in cellular and infection microbiology · 2024Article
- John Squire and the myosin thick filament structure in muscle.Journal of muscle research and cell motility · 2023Review
- ChIP-seq profiling of H3K4me3 and H3K27me3 in an invasive insect,Frontiers in genetics · 2023Article
- Genome-wide transcriptomic changes reveal the genetic pathways involved in insect migration.Molecular ecology · 2022Article
- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
- Contiguity and Structural Impacts of a Non-Myosin Protein within the Thick Filament Myosin Layers.Biology · 2021Article
- Secondary Structure of the Novel Myosin Binding Domain WYR and Implications within Myosin Structure.Biology · 2021Article
- The myosin II coiled-coil domain atomic structure in its native environment.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The actin polymerization factor Diaphanous and the actin severing protein Flightless I collaborate to regulate sarcomere size.Developmental biology · 2021Article
- Aedes aegypti post-emergence transcriptome: Unveiling the molecular basis for the hematophagic and gonotrophic capacitation.PLoS neglected tropical diseases · 2021Article
- CRISPR/Cas9 knockout of female-biased genes AeAct-4 or myo-fem in Ae. aegypti results in a flightless phenotype in female, but not male mosquitoes.PLoS neglected tropical diseases · 2020Article
- CryoEM structure ofLife science alliance · 2020Article
- Review
- The genes expression difference between winged and wingless bird cherry-oat aphid Rhopalosiphum padi based on transcriptomic data.Scientific reports · 2019Article
- Imaging neural activity in the ventral nerve cord of behaving adult Drosophila.Nature communications · 2018Article
- Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flightin is a multiply phosphorylated, 20-kD myofibrillar protein found in Drosophila indirect flight muscles (IFM). Previous work suggests that flightin plays an essential, as yet undefined, role in normal sarcomere structure and contractile activity. Here we show that flightin is associated with thick filaments where it is likely to interact with the myosin rod. We have created a null mutation for flightin, fln(0), that results in loss of flight ability but has no effect on fecundity or viability. Electron microscopy comparing pupa and adult fln(0) IFM shows that sarcomeres, and thick and thin filaments in pupal IFM, are 25-30% longer than in wild type. fln(0) fibers are abnormally wavy, but sarcomere and myotendon structure in pupa are otherwise normal. Within the first 5 h of adult life and beginning of contractile activity, IFM fibers become disrupted as thick filaments and sarcomeres are variably shortened, and myofibrils are ruptured at the myotendon junction. Unusual empty pockets and granular material interrupt the filament lattice of adult fln(0) sarcomeres. Site-specific cleavage of myosin heavy chain occurs during this period. That myosin is cleaved in the absence of flightin is consistent with the immunolocalization of flightin on the thick filament and biochemical and genetic evidence suggesting it is associated with the myosin rod. Our results indicate that flightin is required for the establishment of normal thick filament length during late pupal development and thick filament stability in adult after initiation of contractile activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.