Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 548182
Title A SOSEKI-based coordinate system interprets global polarity cues in Arabidopsis
Author(s) Yoshida, Saiko; Schuren, Alja van der; Dop, Maritza van; Galen, Luc van; Saiga, Shunsuke; Adibi, Milad; Möller, Barbara; Hove, Colette A. ten; Marhavy, Peter; Smith, Richard; Friml, Jiri; Weijers, Dolf
Source Nature Plants 5 (2019)2. - ISSN 2055-026X - p. 160 - 166.
DOI https://doi.org/10.1038/s41477-019-0363-6
Department(s) Biochemistry
BBP Bioconversion
EPS
Publication type Refereed Article in a scientific journal
Publication year 2019
Abstract

Multicellular development requires coordinated cell polarization relative to body axes, and translation to oriented cell division 1–3 . In plants, it is unknown how cell polarities are connected to organismal axes and translated to division. Here, we identify Arabidopsis SOSEKI proteins that integrate apical–basal and radial organismal axes to localize to polar cell edges. Localization does not depend on tissue context, requires cell wall integrity and is defined by a transferrable, protein-specific motif. A Domain of Unknown Function in SOSEKI proteins resembles the DIX oligomerization domain in the animal Dishevelled polarity regulator. The DIX-like domain self-interacts and is required for edge localization and for influencing division orientation, together with a second domain that defines the polar membrane domain. Our work shows that SOSEKI proteins locally interpret global polarity cues and can influence cell division orientation. Furthermore, this work reveals that, despite fundamental differences, cell polarity mechanisms in plants and animals converge on a similar protein domain.

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