ArticleThe Journal of biological chemistry2013
Drosophila homologues of adenomatous polyposis coli (APC) and the formin diaphanous collaborate by a conserved mechanism to stimulate actin filament assembly.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- CKAP5 enables formation of persistent actin bundles templated by dynamically instable microtubules.Current biology : CB · 2024Article
- APC-driven actin nucleation powers collective cell dynamics in colorectal cancer cells.iScience · 2023Article
- The conserved Pelado/ZSWIM8 protein regulates actin dynamics by promoting linear actin filament polymerization.Life science alliance · 2022Article
- The role of APC-mediated actin assembly in microtubule capture and focal adhesion turnover.The Journal of cell biology · 2019Article
- Wnt/Beta-Catenin Signaling Regulation and a Role for Biomolecular Condensates.Developmental cell · 2019Review
- 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
- Adenomatous polyposis coli nucleates actin assembly to drive cell migration and microtubule-induced focal adhesion turnover.The Journal of cell biology · 2017Article
- Cytoskeletal social networking in the growth cone: How +TIPs mediate microtubule-actin cross-linking to drive axon outgrowth and guidance.Cytoskeleton (Hoboken, N.J.) · 2016Review
- 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
- Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.Developmental cell · 2014Article
- Formin' cellular structures: Physiological roles of Diaphanous (Dia) in actin dynamics.Communicative & integrative biology · 2013Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
backgroundVertebrate APC collaborates with Dia through its Basic domain to assemble actin filaments.
resultsDespite limited sequence homology between the vertebrate and Drosophila APC Basic domains, Drosophila APC1 collaborates with Dia to stimulate actin assembly in vitro.
conclusionThe mechanism of actin assembly is highly conserved over evolution. SIGNIFICANCE: APC-Dia collaborations may be crucial in a wide range of animal cells. Adenomatous polyposis coli (APC) is a large multidomain protein that regulates the cytoskeleton. Recently, it was shown that vertebrate APC through its Basic domain directly collaborates with the formin mDia1 to stimulate actin filament assembly in the presence of nucleation barriers. However, it has been unclear whether these activities extend to homologues of APC and Dia in other organisms. Drosophila APC and Dia are each required to promote actin furrow formation in the syncytial embryo, suggesting a potential collaboration in actin assembly, but low sequence homology between the Basic domains of Drosophila and vertebrate APC has left their functional and mechanistic parallels uncertain. To address this question, we purified Drosophila APC1 and Dia and determined their individual and combined effects on actin assembly using both bulk fluorescence assays and total internal reflection fluorescence microscopy. Our data show that APC1, similar to its vertebrate homologue, bound to actin monomers and nucleated and bundled filaments. Further, Drosophila Dia nucleated actin assembly and protected growing filament barbed ends from capping protein. Drosophila APC1 and Dia directly interacted and collaborated to promote actin assembly in the combined presence of profilin and capping protein. Thus, despite limited sequence homology, Drosophila and vertebrate APCs exhibit highly related activities and mechanisms and directly collaborate with formins. These results suggest that APC-Dia interactions in actin assembly are conserved and may underlie important in vivo functions in a broad range of animal phyla.
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