6rsn | pdb_00006rsn

SOSEKI polymerising domain (SOK4 D85A mutant)

spinqualitylabelsall models 6rsn, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rsn is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: MSE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SOK4_ARATH SOSEKI proteins (SOK1-5) locally interpret global polarity cues and can influence cell division orientation to coordinate cell polarization relative to body axes, probably by guiding ANGUSTIFOLIA (AN) polarized localization (PubMed:30737509). Positive regulator of auxin (indole-3-acetic acid, IAA) biosynthesis and signaling pathway leading to the modulation of seedling growth, plant and inflorescence development (PubMed:31207460). Negative regulator of stress responses (e.g. salinity and osmotic stress) (PubMed:31207460). Publication Abstract from PubMed 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. DIX Domain Polymerization Drives Assembly of Plant Cell Polarity Complexes.,van Dop M, Fiedler M, Mutte S, de Keijzer J, Olijslager L, Albrecht C, Liao CY, Janson ME, Bienz M, Weijers D Cell. 2020 Feb 6;180(3):427-439.e12. doi: 10.1016/j.cell.2020.01.011. Epub 2020, Jan 30. PMID:32004461 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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