A receptor heteromer mediates the male perception of female attractants in plants

Nature. 2016 Mar 10;531(7593):241-4. doi: 10.1038/nature16975. Epub 2016 Feb 10.

Abstract

Sexual reproduction requires recognition between the male and female gametes. In flowering plants, the immobile sperms are delivered to the ovule-enclosed female gametophyte by guided pollen tube growth. Although the female gametophyte-secreted peptides have been identified to be the chemotactic attractant to the pollen tube, the male receptor(s) is still unknown. Here we identify a cell-surface receptor heteromer, MDIS1-MIK, on the pollen tube that perceives female attractant LURE1 in Arabidopsis thaliana. MDIS1, MIK1 and MIK2 are plasma-membrane-localized receptor-like kinases with extracellular leucine-rich repeats and an intracellular kinase domain. LURE1 specifically binds the extracellular domains of MDIS1, MIK1 and MIK2, whereas mdis1 and mik1 mik2 mutant pollen tubes respond less sensitively to LURE1. Furthermore, LURE1 triggers dimerization of the receptors and activates the kinase activity of MIK1. Importantly, transformation of AtMDIS1 to the sister species Capsella rubella can partially break down the reproductive isolation barrier. Our findings reveal a new mechanism of the male perception of the female attracting signals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / genetics
  • Arabidopsis / metabolism*
  • Arabidopsis / physiology
  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Capsella / genetics
  • Capsella / metabolism
  • Capsella / physiology
  • Cell Membrane / metabolism
  • Mutation
  • Ovule / metabolism
  • Phenotype
  • Phosphotransferases / chemistry
  • Phosphotransferases / genetics
  • Phosphotransferases / metabolism*
  • Pollen Tube / genetics
  • Pollen Tube / growth & development
  • Pollen Tube / metabolism
  • Protein Kinases / genetics
  • Protein Kinases / metabolism
  • Protein Multimerization
  • Protein Serine-Threonine Kinases
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Receptors, Cell Surface / chemistry
  • Receptors, Cell Surface / genetics
  • Receptors, Cell Surface / metabolism*
  • Reproduction
  • Signal Transduction*

Substances

  • Arabidopsis Proteins
  • MDIS1 protein, Arabidopsis
  • Receptors, Cell Surface
  • MIK1 protein, Arabidopsis
  • Phosphotransferases
  • Protein Kinases
  • MDIS2 protein, Arabidopsis
  • MIK2 protein, Arabidopsis
  • Protein Serine-Threonine Kinases