Journal
NATURE
Volume 473, Issue 7347, Pages 380-U564Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature10070
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Funding
- Swiss National Science Foundation
- European Research Council (ERC)
- Belgian Interuniversity Attraction Poles program [IUAP VI/33]
- Ghent University
- Roche Research Foundation
- Marie-Curie IEF grant
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Polarized epithelia are fundamental to multicellular life. In animal epithelia, conserved junctional complexes establish membrane diffusion barriers, cellular adherence and sealing of the extracellular space(1). Plant cellular barriers are of independent evolutionary origin. The root endodermis strongly resembles a polarized epithelium and functions in nutrient uptake and stress resistance(2). Its defining features are the Casparian strips, belts of specialized cell wall material that generate an extracellular diffusion barrier(2). The mechanisms localizing Casparian strips are unknown. Here we identify and characterize a family of transmembrane proteins of previously unknown function. These 'CASPs' (Casparian strip membrane domain proteins) specifically mark a membrane domain that predicts the formation of Casparian strips. CASP1 displays numerous features required for a constituent of a plant junctional complex: it forms complexes with other CASPs; it becomes immobile upon localization; and it sediments like a large polymer. CASP double mutants display disorganized Casparian strips, demonstrating a role for CASPs in structuring and localizing this cell wall modification. To our knowledge, CASPs are the first molecular factors that are shown to establish a plasma membrane and extracellular diffusion barrier in plants, and represent a novel way of epithelial barrier formation in eukaryotes.
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