ArticleThe Journal of cell biology2001
Thin filaments elongate from their pointed ends during myofibril assembly 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 48 papers.
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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
48 citing papers in PubMed, 83 citations in OpenAlex.
- Signalling networks orchestrating the development of Drosophila indirect flight muscles.Histochemistry and cell biology · 2026Review
- TET exhibits enzymatic-independent and-dependent functions during Drosophila flight muscle development and aging.Skeletal muscle · 2025Article
- Developmental remodelling ofOpen biology · 2025Article
- 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
- Review
- Drosophila Tropomodulin is required for multiple actin-dependent processes within developing myofibers.Development (Cambridge, England) · 2023Article
- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
- Mutual dependence between tropomodulin and tropomyosin in the regulation of sarcomeric actin assembly in Caenorhabditis elegans striated muscle.European journal of cell biology · 2022Article
- Geometric basis of action potential of skeletal muscle cells and neurons.Open life sciences · 2022Review
- Natural variation in the regulation of neurodevelopmental genes modifies flight performance in Drosophila.PLoS genetics · 2021Article
- The actin polymerization factor Diaphanous and the actin severing protein Flightless I collaborate to regulate sarcomere size.Developmental biology · 2021Article
- An insight on Drosophila myogenesis and its assessment techniques.Molecular biology reports · 2020Review
- A Novel Mechanism for Activation of Myosin Regulatory Light Chain by Protein Kinase C-Delta inGenetics · 2020Article
- Cofilin Loss in Drosophila Muscles Contributes to Muscle Weakness through Defective Sarcomerogenesis during Muscle Growth.Cell reports · 2020Article
- Review
- Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes.The Journal of cell biology · 2020Article
- Commentary: Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes.Frontiers in cell and developmental biology · 2020Article
- Novel functions for integrin-associated proteins revealed by analysis of myofibril attachment ineLife · 2018Article
- Chaperones and the Proteasome System: Regulating the Construction and Demolition of Striated Muscle.International journal of molecular sciences · 2017Review
- Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles.Biophysical journal · 2017Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Tropomodulin (Tmod) is an actin pointed-end capping protein that regulates actin dynamics at thin filament pointed ends in striated muscle. Although pointed-end capping by Tmod controls thin filament lengths in assembled myofibrils, its role in length specification during de novo myofibril assembly is not established. We used the Drosophila Tmod homologue, sanpodo (spdo), to investigate Tmod's function during muscle development in the indirect flight muscle. SPDO was associated with the pointed ends of elongating thin filaments throughout myofibril assembly. Transient overexpression of SPDO during myofibril assembly irreversibly arrested elongation of preexisting thin filaments. However, the lengths of thin filaments assembled after SPDO levels had declined were normal. Flies with a preponderance of abnormally short thin filaments were unable to fly. We conclude that: (a) thin filaments elongate from their pointed ends during myofibril assembly; (b) pointed ends are dynamically capped at endogenous levels of SPDO so as to allow elongation; (c) a transient increase in SPDO levels during myofibril assembly converts SPDO from a dynamic to a permanent cap; and (d) developmental regulation of pointed-end capping during myofibril assembly is crucial for specification of final thin filament lengths, myofibril structure, and muscle function.
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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.