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Mol Biol Cell 2019 Jan 01;301:82-95. doi: 10.1091/mbc.E18-02-0133.
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Comprehensive analysis of formin localization in Xenopus epithelial cells.

Higashi T , Stephenson RE , Miller AL .

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.

PubMed ID: 30379611
PMC ID: PMC6337911
Article link: Mol Biol Cell
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: daam1 daam2 diaph1 diaph2 diaph3 fhdc1 fhod1 fhod3 fmn1 fmn2 fmnl1 fmnl2 fmnl3 grid2ip inf2 plekha7 rho
GO keywords: cell-cell junction assembly [+]

Article Images: [+] show captions
References [+] :
ALFERT, The development of polysomaty in rat liver. 2000, Pubmed