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

  • Yan Zhuang
  • , Daqing Zuo
  • , Yihan Tao
  • , Huaqing Cai
  • , Lei Li

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

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 CSDMand 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 CSDMto provide bidirectional positional information that guides precise CS lignification.

Original languageEnglish
Pages (from-to)15400-15402
Number of pages3
JournalProceedings of the National Academy of Sciences of the United States of America
Volume117
Issue number27
DOIs
StatePublished - 7 Jul 2020
Externally publishedYes

Keywords

  • Casparian strip
  • Copper
  • Laccase
  • Lignin
  • Positional information

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