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Visualizing Lignification Dynamics in Plants with Click Chemistry: Dual Labeling is BLISS!
Published on: January 26, 2018
Laccase3-based extracellular domain provides possible positional information for directing Casparian strip formation
Yan Zhuang1,2, Daqing Zuo1, Yihan Tao1
1State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences and School of Advanced Agricultural Sciences, Peking University, 100871 Beijing, China.
Abstract:
The Casparian strip (CS) is a tight junction-like structure formed by lignin impregnation on the walls of endodermal cells in plant roots. The CS membrane domain (CSDM), demarked by the CASP proteins, is important for orienting lignification enzymes. Here, we report that an endodermis-expressed multicopper oxidase, LACCASE3 (LAC3) in Arabidopsis, locates to the interface between lignin domains and the cell wall during early CS development prior to CASP1 localizing to CSDM and eventually flanks the mature CS. Pharmacological perturbation of LAC3 causes dispersed localization of CASP1 and compensatory ectopic lignification. These results support the existence of a LAC3-based CS wall domain which coordinates with CSDM to provide bidirectional positional information that guides precise CS lignification.
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