ArticleDevelopment (Cambridge, England)2009
A novel role for an APC2-Diaphanous complex in regulating actin organization in Drosophila.
Article in Development (Cambridge, England), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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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Who cites it
28 citing papers in PubMed, 39 citations in OpenAlex.
- Bitesize bundles F-actin and influences actin remodeling in syncytial Drosophila embryo development.The Journal of cell biology · 2026Article
- Molecular Dissection of DAAM Function during Axon Growth in Drosophila Embryonic Neurons.Cells · 2022Article
- The actin polymerization factor Diaphanous and the actin severing protein Flightless I collaborate to regulate sarcomere size.Developmental biology · 2021Article
- EB1 Directly Regulates APC-Mediated Actin Nucleation.Current biology : CB · 2020Article
- Par-1 controls the composition and growth of cortical actin caps duringThe Journal of cell biology · 2019Article
- The role of APC-mediated actin assembly in microtubule capture and focal adhesion turnover.The Journal of cell biology · 2019Article
- The Crk adapter protein is essential forMolecular biology of the cell · 2019Article
- Wnt/Beta-Catenin Signaling Regulation and a Role for Biomolecular Condensates.Developmental cell · 2019Review
- Coordination of Embryogenesis by the Centrosome in Drosophila melanogaster.Results and problems in cell differentiation · 2019Review
- APC2 controls dendrite development by promoting microtubule dynamics.Nature communications · 2018Article
- APC2 associates with the actin cortex through a multipart mechanism to regulate cortical actin organization and dynamics in the Drosophila ovary.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Identification of Proteins Required for Precise Positioning of Apc2 in Dendrites.G3 (Bethesda, Md.) · 2018Article
- Adenomatous polyposis coli nucleates actin assembly to drive cell migration and microtubule-induced focal adhesion turnover.The Journal of cell biology · 2017Article
- Proteomic analysis reveals APC-dependent post-translational modifications and identifies a novel regulator of β-catenin.Development (Cambridge, England) · 2016Article
- Syndapin promotes pseudocleavage furrow formation by actin organization in the syncytial Drosophila embryo.Molecular biology of the cell · 2016Article
- An mDia1-INF2 formin activation cascade facilitated by IQGAP1 regulates stable microtubules in migrating cells.Molecular biology of the cell · 2016Article
- Pebble/ECT2 RhoGEF negatively regulates the Wingless/Wnt signaling pathway.Development (Cambridge, England) · 2013Article
- Formin' cellular structures: Physiological roles of Diaphanous (Dia) in actin dynamics.Communicative & integrative biology · 2013Review
- APC2 and Axin promote mitotic fidelity by facilitating centrosome separation and cytoskeletal regulation.Development (Cambridge, England) · 2013Article
- Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleation.The Journal of cell biology · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The rearrangement of cytoskeletal elements is essential for many cellular processes. The tumor suppressor Adenomatous polyposis coli (APC) affects the function of microtubules and actin, but the mechanisms by which it does so are not well understood. Here we report that Drosophila syncytial embryos null for Apc2 display defects in the formation and extension of pseudocleavage furrows, which are cortical actin structures important for mitotic fidelity in early embryos. Furthermore, we show that the formin Diaphanous (DIA) functions with APC2 in this process. Colocalization of APC2 and DIA peaks during furrow extension, and localization of APC2 to furrows is DIA-dependent. Furthermore, APC2 binds DIA directly through a region of APC2 not previously shown to interact with DIA-related formins. Consistent with these results, reduction of dia enhances actin defects in Apc2 mutant embryos. Thus, an APC2-DIA complex appears crucial for actin furrow extension in the syncytial embryo. Interestingly, EB1, a microtubule +TIP and reported partner of vertebrate APC and DIA1, may not function with APC2 and DIA in furrow extension. Finally, whereas DIA-related formins are activated by Rho family GTPases, our data suggest that the APC2-DIA complex might be independent of RHOGEF2 and RHO1. Furthermore, although microtubules play a role in furrow extension, our analysis suggests that APC2 and DIA function in a novel complex that affects actin directly, rather than through an effect on microtubules.
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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.