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- W2898888650 abstract "Reorganization of the actin cytoskeleton is crucial for cellular processes, including cytokinesis and cell–cell junction remodeling. Formins are conserved processive actin-polymerizing machines that regulate actin dynamics by nucleating, elongating, and bundling linear actin filaments. Because the formin family is large, with at least 15 members in vertebrates, there have not been any comprehensive studies examining formin localization and function within a common cell type. Here, we characterized the localization of all 15 formins in epithelial cells of Xenopus laevis gastrula-stage embryos. Dia1 and Dia2 localized to tight junctions, while Fhod1 and Fhod3 localized to adherens junctions. Only Dia3 strongly localized at the cytokinetic contractile ring. The Diaphanous inhibitory domain–dimerization domain (DID-DD) region of Dia1 was sufficient for Dia1 localization, and overexpression of a Dia1 DID-DD fragment competitively removed Dia1 and Dia2 from cell–cell junctions. In Dia1 DID-DD–overexpressing cells, Dia1 and Dia2 were mislocalized to the contractile ring, and cells exhibited increased cytokinesis failure. This work provides a comprehensive analysis of the localization of all 15 vertebrate formins in epithelial cells and suggests that misregulated formin localization results in epithelial cytokinesis failure." @default.
- W2898888650 created "2018-11-09" @default.
- W2898888650 creator A5048948807 @default.
- W2898888650 creator A5067306006 @default.
- W2898888650 creator A5073710580 @default.
- W2898888650 date "2019-01-01" @default.
- W2898888650 modified "2023-09-23" @default.
- W2898888650 title "Comprehensive analysis of formin localization in<i>Xenopus</i>epithelial cells" @default.
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- W2898888650 doi "https://doi.org/10.1091/mbc.e18-02-0133" @default.
- W2898888650 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6337911" @default.
- W2898888650 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30379611" @default.
- W2898888650 hasPublicationYear "2019" @default.
- W2898888650 type Work @default.