Laccase3-based extracellular domain provides possible positional information for directing Casparian strip formation in <i>Arabidopsis</i>.
basic_science · Level V
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- Record sourced from PubMed, PMID 32571955.
- Also identified by DOI 10.1073/pnas.2005429117 and PMC identifier 7355012.
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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<sup>M</sup>), demarked by the CASP proteins, is important for orienting lignification enzymes. Here, we report that an endodermis-expressed multicopper oxidase, LACCASE3 (LAC3) in <i>Arabidopsis</i>, locates to the interface between lignin domains and the cell wall during early CS development prior to CASP1 localizing to CSD<sup>M</sup> 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<sup>M</sup> to provide bidirectional positional information that guides precise CS lignification.
Medical subject headings
- Arabidopsis
- Arabidopsis Proteins
- Laccase
- Membrane Proteins
- Plant Roots