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Laccase3-based extracellular domain provides possible positional information for directing Casparian strip formation in Arabidopsis.

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 (CSD^M), 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 CSD^M 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 CSD^M to provide bidirectional positional information that guides precise CS lignification.

SUBMITTER: Zhuang Y

PROVIDER: S-EPMC7355012 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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Laccase3-based extracellular domain provides possible positional information for directing Casparian strip formation in Arabidopsis.

Zhuang Yan Y Zuo Daqing D Tao Yihan Y Cai Huaqing H Li Lei L

Proceedings of the National Academy of Sciences of the United States of America 20200622 27

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< ...[more]

PMID: 32571955

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