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

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 mu...

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Detalles Bibliográficos
Autores principales: Zhuang, Yan, Zuo, Daqing, Tao, Yihan, Cai, Huaqing, Li, Lei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7355012/
https://www.ncbi.nlm.nih.gov/pubmed/32571955
http://dx.doi.org/10.1073/pnas.2005429117
Descripción
Sumario: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.