A protein phosphatase 2A complex spatially controls plant cell division

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Spinner, Lara | Gadeyne, Astrid | Belcram, Katia | Goussot, Magali | Moison, Michaël | Duroc, Yann | Eeckhout, Dominique | de Winne, Nancy | Schaefer, Estelle | van de Slijke, Eveline | Persiau, Geert | Witters, Erwin | Gevaert, Kris | de Jaeger, Geert | Bouchez, David | van Damme, Daniel | Pastuglia, Martine

Edité par CCSD ; Nature Publishing Group -

In the absence of cell migration, the orientation of cell divisions is crucial for body plan determination in plants. The position of the division plane in plant cells is set up premitotically via a transient cytoskeletal array, the preprophase band, which precisely delineates the cortical plane of division. Here we describe a protein complex that targets protein phosphatase 2A activity to microtubules, regulating the transition from the interphase to the premitotic microtubule array. This complex, which comprises TONNEAU1 and a PP2A heterotrimeric holoenzyme with FASS as regulatory subunit, is recruited to the cytoskeleton via the TONNEAU1-recruiting motif family of proteins. Despite the acentrosomal nature of plant cells, all members of this complex share similarity with animal centrosomal proteins involved in ciliary and centriolar/centrosomal functions, revealing an evolutionary link between the cortical cytoskeleton of plant cells and microtubule organizers in other eukaryotes.

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