6RSN

SOSEKI polymerising domain (SOK4 D85A mutant)

6RSN の概要

• エントリーDOI: 10.2210/pdb6rsn/pdb
• 関連するPDBエントリー: 4wip
• 分子名称: UPSTREAM OF FLC-like protein (DUF966), SULFATE ION (3 entities in total)
• 機能のキーワード: polymeriser, plant protein, ubiquitin-like fold, polarity protein, signaling protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11234.52

構造登録者

Fiedler, M.,Bienz, M. (登録日: 2019-05-21, 公開日: 2020-01-29, 最終更新日: 2020-02-19)

主引用文献

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

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: 32004461
DOI: 10.1016/j.cell.2020.01.011

実験手法

X-RAY DIFFRACTION (1.7 Å)