ArticlePLoS genetics2015
The Formin Diaphanous Regulates Myoblast Fusion through Actin Polymerization and Arp2/3 Regulation.
Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 40 citations in OpenAlex.
- Signalling networks orchestrating the development of Drosophila indirect flight muscles.Histochemistry and cell biology · 2026Review
- ARP2/3 protein complex regulates myoblast proliferation, morphology, migration, and fusion during embryonic chick skeletal myogenesis.In vitro cellular & developmental biology. Animal · 2026Article
- The Innovative Role of Nuclear Receptor Interaction Protein in Orchestrating Invadosome Formation for Myoblast Fusion.Journal of cachexia, sarcopenia and muscle · 2024Article
- Machine learning inference of continuous single-cell state transitions during myoblast differentiation and fusion.Molecular systems biology · 2024Article
- The Abl-interactor Abi suppresses the function of the BRAG2 GEF family member Schizo.Biology open · 2024Article
- Review
- Scar/WAVE has Rac GTPase-independent functions during cell wound repair.Scientific reports · 2023Article
- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
- Cytonemes coordinate asymmetric signaling and organization in the Drosophila muscle progenitor niche.Nature communications · 2022Article
- Review
- miRNA mediated downregulation of cyclase-associated protein 1 (CAP1) is required for myoblast fusion.Frontiers in cell and developmental biology · 2022Article
- Development of the indirect flight muscles of Aedes aegypti, a main arbovirus vector.BMC developmental biology · 2021Article
- The actin polymerization factor Diaphanous and the actin severing protein Flightless I collaborate to regulate sarcomere size.Developmental biology · 2021Article
- Reverse-engineering forces responsible for dynamic clustering and spreading of multiple nuclei in developing muscle cells.Molecular biology of the cell · 2020Article
- The Arp2/3 complex and the formin, Diaphanous, are both required to regulate the size of germline ring canals in the developing egg chamber.Developmental biology · 2020Article
- WASP family proteins regulate the mobility of the B cell receptor during signaling activation.Nature communications · 2020Article
- Review
- The fusogenic synapse at a glance.Journal of cell science · 2019Review
- Cytoplasmic sequestration of the RhoA effector mDiaphanous1 by Prohibitin2 promotes muscle differentiation.Scientific reports · 2019Article
- Conserved pathway activation following xenogeneic, heterotypic fusion.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The formation of multinucleated muscle cells through cell-cell fusion is a conserved process from fruit flies to humans. Numerous studies have shown the importance of Arp2/3, its regulators, and branched actin for the formation of an actin structure, the F-actin focus, at the fusion site. This F-actin focus forms the core of an invasive podosome-like structure that is required for myoblast fusion. In this study, we find that the formin Diaphanous (Dia), which nucleates and facilitates the elongation of actin filaments, is essential for Drosophila myoblast fusion. Following cell recognition and adhesion, Dia is enriched at the myoblast fusion site, concomitant with, and having the same dynamics as, the F-actin focus. Through analysis of Dia loss-of-function conditions using mutant alleles but particularly a dominant negative Dia transgene, we demonstrate that reduction in Dia activity in myoblasts leads to a fusion block. Significantly, no actin focus is detected, and neither branched actin regulators, SCAR or WASp, accumulate at the fusion site when Dia levels are reduced. Expression of constitutively active Dia also causes a fusion block that is associated with an increase in highly dynamic filopodia, altered actin turnover rates and F-actin distribution, and mislocalization of SCAR and WASp at the fusion site. Together our data indicate that Dia plays two roles during invasive podosome formation at the fusion site: it dictates the level of linear F-actin polymerization, and it is required for appropriate branched actin polymerization via localization of SCAR and WASp. These studies provide new insight to the mechanisms of cell-cell fusion, the relationship between different regulators of actin polymerization, and invasive podosome formation that occurs in normal development and in disease.
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Registered trials
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