한빛사 논문
Abstract
Yuree Lee,1 Maria C. Rubio,1,2 Julien Alassimone,1,3 and Niko Geldner1,*
1Department of Plant Molecular Biology, University of Lausanne, UNIL-Sorge, Biophore Building, 1015 Lausanne, Switzerland
2Departamento de Nutricio´ n Vegetal, Estacio´ n Experimental de Aula Dei, Consejo Superior de Investigaciones Cientı´ficas, Apdo 13034, 50080 Zaragoza, Spain
3Present address: Department of Biology, Stanford University, 371 Serra Mall, Stanford, CA 94305-5020, USA
*Correspondence: Niko Geldner
Summary
The precise localization of extracellular matrix and cell wall components is of critical importance for multicellular organisms. Lignin is a major cell wall modification that often forms intricate subcellular patterns that are central to cellular function. Yet the mechanisms of lignin polymerization and the subcellular precision of its formation remain enigmatic. Here, we show that the Casparian strip, a lignin-based, paracellular diffusion barrier in plants, forms as a precise, median ring by the concerted action of a specific, localized NADPH oxidase, brought into proximity of localized peroxidases through the action of Casparian strip domain proteins (CASPs). Our findings in Arabidopsis provide a simple mechanistic model of how plant cells regulate lignin formation with subcellular precision. We speculate that scaffolding of NADPH oxidases to the downstream targets of the reactive oxygen species (ROS) that they produce might be a widespread mechanism to ensure specificity and subcellular precision of ROS action within the extracellular matrix.
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