Plant formin AtFH5 is an evolutionarily conserved actin nucleator involved in cytokinesis.

Formins are actin-organizing proteins that are involved in cytokinesis and cell polarity. In the plant Arabidopsis thaliana, there are more than 20 formin homologues, all of which have unknown roles. In this study, we characterize specific cellular and molecular functions of the Arabidopsis formin AtFH5. Despite the low identity of AtFH5 to yeast and mammalian formins, the AtFH5 protein interacts with the barbed end of actin filaments and nucleates actin-filament polymerization in vitro, as is the case in yeast and mammals. In vivo, the AtFH5-GFP fusion protein localizes to the cell plate, a plant-specific membranous component that is assembled at the plane of cell division. Consistent with these data, loss of function of atfh5 compromises cytokinesis in the seed endosperm. Furthermore, endogenous AtFH5 transcripts accumulate in the posterior pole of the endosperm and loss of function of atfh5 perturbs proper morphogenesis of the endosperm posterior pole. Although cytokinesis in animals, yeast and plants occurs through morphologically distinct mechanisms, our study finds that formin recruitment to sites of actin assembly is a common feature of cell division among eukaryotes.

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