title: Polarly localized kinase SGN1 is required for Casparian strip integrity and positioning.
abstract: Casparian strips are precisely localized and aligned ring-like cell wall modifications in the root of all higher plants. They set up an extracellular diffusion barrier analogous to animal tight junctions, and are crucial for maintaining the homeostatic capacity of plant roots. Casparian strips become localized because of the formation of a highly stable plasma membrane domain, consisting of a family of small transmembrane proteins called Casparian strip membrane domain proteins (CASPs). Here we report a large-scale forward genetic screen directly visualizing endodermal barrier function, which allowed us to identify factors required for the formation and integrity of Casparian strips. We present the identification and characterization of one of the mutants, schengen1 (sgn1), a receptor-like cytoplasmic kinase that we show localizes in a strictly polar fashion to the outer plasma membrane of endodermal cells and is required for the positioning and correct formation of the centrally located CASP domain.
authors.affiliation: Department of Plant Molecular Biology, Biophore, Campus UNIL-Sorge, University of Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Julien
authors.identifier: 0000-0002-8118-2605
authors.initials: J
authors.lastname: Alassimone
authors.affiliation: Department of Plant Molecular Biology, Biophore, Campus UNIL-Sorge, University of Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Satoshi
authors.initials: S
authors.lastname: Fujita
authors.affiliation: Department of Plant Molecular Biology, Biophore, Campus UNIL-Sorge, University of Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Verónica G
authors.initials: VG
authors.lastname: Doblas
authors.affiliation: Department of Plant Molecular Biology, Biophore, Campus UNIL-Sorge, University of Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Maritza
authors.initials: M
authors.lastname: van Dop
authors.affiliation: Department of Plant Molecular Biology, Biophore, Campus UNIL-Sorge, University of Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Marie
authors.initials: M
authors.lastname: Barberon
authors.affiliation: Department of Plant Molecular Biology, Biophore, Campus UNIL-Sorge, University of Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Lothar
authors.initials: L
authors.lastname: Kalmbach
authors.affiliation: Department of Plant Molecular Biology, Biophore, Campus UNIL-Sorge, University of Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Joop E M
authors.initials: JE
authors.lastname: Vermeer
authors.affiliation: Department of Plant Molecular Biology, Biophore, Campus UNIL-Sorge, University of Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Nelson
authors.initials: N
authors.lastname: Rojas-Murcia
authors.affiliation: Department of Plant Molecular Biology, Biophore, Campus UNIL-Sorge, University of Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Luca
authors.initials: L
authors.lastname: Santuari
authors.affiliation: Department of Plant Molecular Biology, Biophore, Campus UNIL-Sorge, University of Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Christian S
authors.identifier: 0000-0003-3203-1058
authors.initials: CS
authors.lastname: Hardtke
authors.affiliation: Department of Plant Molecular Biology, Biophore, Campus UNIL-Sorge, University of Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Niko
authors.initials: N
authors.lastname: Geldner
mesh_terms: D017360:Arabidopsis / Q000235:genetics*; D029681:Arabidopsis Proteins / Q000235:genetics* / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism*; D004058:Diffusion; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D008565:Membrane Proteins