ArticleThe Journal of cell biology2001
Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle.
Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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47 citing papers in PubMed, 90 citations in OpenAlex.
- Nx3 Is a Z-Disk Structural and Signaling Hub That Is Reduced in Heart Failure.Circulation research · 2026Article
- Fine-tuning striated muscle performance: conserved sarcomere-level mechanisms across insect and vertebrate systems.Frontiers in physiology · 2026Review
- Two Forms of Thick Filament in the Flight Muscle ofInternational journal of molecular sciences · 2024Article
- Peripheral thickening of the sarcomeres and pointed end elongation of the thin filaments are both promoted by SALS and its formin interaction partners.PLoS genetics · 2024Article
- The cryo-EM 3D image reconstruction of isolated Lethocerus indicus Z-discs.Journal of muscle research and cell motility · 2023Review
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- Disruption of Drosophila larval muscle structure and function by UNC45 knockdown.BMC molecular and cell biology · 2021Article
- Molecular Characterisation of Titin N2A and Its Binding of CARP Reveals a Titin/Actin Cross-linking Mechanism.Journal of molecular biology · 2021Article
- Article
- Localization of the Elastic Proteins in the Flight Muscle ofInternational journal of molecular sciences · 2020Article
- Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes.The Journal of cell biology · 2020Article
- Through thick and thin: dual regulation of insect flight muscle and cardiac muscle compared.Journal of muscle research and cell motility · 2019Review
- Filamin actin-binding and titin-binding fulfill distinct functions in Z-disc cohesion.PLoS genetics · 2017Article
- Structure of isolated Z-disks from honeybee flight muscle.Journal of muscle research and cell motility · 2017Article
- Elastic proteins in the flight muscle of Manduca sexta.Archives of biochemistry and biophysics · 2015Article
- Distinct genetic programs guide Drosophila circular and longitudinal visceral myoblast fusion.BMC cell biology · 2014Article
- An embryonic myosin converter domain influences Drosophila indirect flight muscle stretch activation, power generation and flight.The Journal of experimental biology · 2014Article
- Molecular analysis of the muscle protein projectin in Lepidoptera.Journal of insect science (Online) · 2013Article
- Mechanical analysis of Drosophila indirect flight and jump muscles.Methods (San Diego, Calif.) · 2012Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kettin is a high molecular mass protein of insect muscle that in the sarcomeres binds to actin and alpha-actinin. To investigate kettin's functional role, we combined immunolabeling experiments with mechanical and biochemical studies on indirect flight muscle (IFM) myofibrils of Drosophila melanogaster. Micrographs of stretched IFM sarcomeres labeled with kettin antibodies revealed staining of the Z-disc periphery. After extraction of the kettin-associated actin, the A-band edges were also stained. In contrast, the staining pattern of projectin, another IFM-I-band protein, was not altered by actin removal. Force measurements were performed on single IFM myofibrils to establish the passive length-tension relationship and record passive stiffness. Stiffness decreased within seconds during gelsolin incubation and to a similar degree upon kettin digestion with mu-calpain. Immunoblotting demonstrated the presence of kettin isoforms in normal Drosophila IFM myofibrils and in myofibrils from an actin-null mutant. Dotblot analysis revealed binding of COOH-terminal kettin domains to myosin. We conclude that kettin is attached not only to actin but also to the end of the thick filament. Kettin along with projectin may constitute the elastic filament system of insect IFM and determine the muscle's high stiffness necessary for stretch activation. Possibly, the two proteins modulate myofibrillar stiffness by expressing different size isoforms.
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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.