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DIX Domain Polymerization Drives Assembly of Plant Cell Polarity Complexes.

Cell. 2020 Feb 06;180(3):427-439.e12. Epub 2020 Jan 30
Maritza van Dop 1 , Marc Fiedler 2 , Sumanth Mutte 1 , Jeroen de Keijzer 3 , Lisa Olijslager 1 , Catherine Albrecht 1 , Che-Yang Liao 1 , Marcel E Janson 3 , Mariann Bienz 4 , Dolf Weijers 5
Maritza van Dop 1 , Marc Fiedler 2 , Sumanth Mutte 1 , Jeroen de Keijzer 3 , Lisa Olijslager 1 , Catherine Albrecht 1 , Che-Yang Liao 1 , Marcel E Janson 3 , Mariann Bienz 4 , Dolf Weijers 5
+ et al

[No authors listed]

Author information
  • 1 Laboratory of Biochemistry, Wageningen University, Stippeneng 4, Wageningen, the Netherlands.
  • 2 MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
  • 3 Laboratory of Cell Biology, Wageningen University, Droevendaalsesteeg 1, Wageningen, the Netherlands.
  • 4 MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: mb2@mrc-lmb.cam.ac.uk.
  • 5 Laboratory of Biochemistry, Wageningen University, Stippeneng 4, Wageningen, the Netherlands. Electronic address: dolf.weijers@wur.nl.

摘要


Cell polarity is fundamental for tissue morphogenesis in multicellular organisms. Plants and animals evolved multicellularity independently, and it is unknown whether their polarity systems are derived from a single-celled ancestor. Planar polarity in animals is conferred by Wnt signaling, an ancient signaling pathway transduced by Dishevelled, which assembles signalosomes by dynamic head-to-tail DIX domain polymerization. In contrast, polarity-determining pathways in plants are elusive. We recently discovered Arabidopsis SOSEKI proteins, which exhibit polar localization throughout development. Here, we identify SOSEKI as ancient polar proteins across land plants. Concentration-dependent polymerization via a bona fide DIX domain allows these to recruit ANGUSTIFOLIA to polar sites, similar to the polymerization-dependent recruitment of signaling effectors by Dishevelled. Cross-kingdom domain swaps reveal functional equivalence of animal and plant DIX domains. We trace DIX domains to unicellular eukaryotes and thus show that DIX-dependent polymerization is an ancient mechanism conserved between kingdoms and central to polarity proteins.

KEYWORDS: DIX domain, SOSEKI, cell polarity, dishevelled, plant development, protein oligomerization, signalosome