6RSN
SOSEKI polymerising domain (SOK4 D85A mutant)
Summary for 6RSN
| Entry DOI | 10.2210/pdb6rsn/pdb |
| Related | 4wip |
| Descriptor | UPSTREAM OF FLC-like protein (DUF966), SULFATE ION (3 entities in total) |
| Functional Keywords | polymeriser, plant protein, ubiquitin-like fold, polarity protein, signaling protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 11234.52 |
| Authors | Fiedler, M.,Bienz, M. (deposition date: 2019-05-21, release date: 2020-01-29, Last modification date: 2020-02-19) |
| Primary citation | van Dop, M.,Fiedler, M.,Mutte, S.,de Keijzer, J.,Olijslager, L.,Albrecht, C.,Liao, C.Y.,Janson, M.E.,Bienz, M.,Weijers, D. DIX Domain Polymerization Drives Assembly of Plant Cell Polarity Complexes. Cell, 180:427-, 2020 Cited by PubMed Abstract: 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. PubMed: 32004461DOI: 10.1016/j.cell.2020.01.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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