ArticleJournal of cell science2023
The oxoglutarate dehydrogenase complex is involved in myofibril growth and Z-disc assembly in Drosophila.
Article in Journal of cell science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 7 citations in OpenAlex.
- HeterozygousJIMD reports · 2026Article
- Analysis of Muscle Structure Using Fluorescently Tagged Proteins in Drosophila melanogaster Femur Muscles.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Proteomic Analysis of Thin Filament Components Elucidates Changes in Spastic Muscle Sarcomere After Stroke.International journal of molecular sciences · 2025Article
- Second harmonic generation of myofibrils exhibits a polarization-resolved "gradient" effect.Biomedical optics express · 2025Article
- Developmental remodelling ofOpen biology · 2025Article
- Filamin protects myofibrils from contractile damage through changes in its mechanosensory region.PLoS genetics · 2024Article
- The alpha-ketoacid dehydrogenase complexes ofmicroPublication biology · 2024Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Myofibrils are long intracellular cables specific to muscles, composed mainly of actin and myosin filaments. The actin and myosin filaments are organized into repeated units called sarcomeres, which form the myofibrils. Muscle contraction is achieved by the simultaneous shortening of sarcomeres, which requires all sarcomeres to be the same size. Muscles have a variety of ways to ensure sarcomere homogeneity. We have previously shown that the controlled oligomerization of Zasp proteins sets the diameter of the myofibril. Here, we looked for Zasp-binding proteins at the Z-disc to identify additional proteins coordinating myofibril growth and assembly. We found that the E1 subunit of the oxoglutarate dehydrogenase complex localizes to both the Z-disc and the mitochondria, and is recruited to the Z-disc by Zasp52. The three subunits of the oxoglutarate dehydrogenase complex are required for myofibril formation. Using super-resolution microscopy, we revealed the overall organization of the complex at the Z-disc. Metabolomics identified an amino acid imbalance affecting protein synthesis as a possible cause of myofibril defects, which is supported by OGDH-dependent localization of ribosomes at the Z-disc.
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Registered trials
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