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

Proc Natl Acad Sci U S A. 2020 Jul 7;117(27):15400-15402. doi: 10.1073/pnas.2005429117. Epub 2020 Jun 22.

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.

Keywords: Casparian strip; copper; laccase; lignin; positional information.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / cytology
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / metabolism*
  • Cell Wall / metabolism
  • Laccase / genetics
  • Laccase / metabolism*
  • Lignin / metabolism
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Plant Roots / cytology
  • Plant Roots / metabolism*
  • Plants, Genetically Modified
  • Protein Domains

Substances

  • Arabidopsis Proteins
  • Membrane Proteins
  • Lignin
  • Laccase