Arabidopsis MAKR5 is a positive effector of BAM3-dependent CLE45 signaling

EMBO Rep. 2016 Aug;17(8):1145-54. doi: 10.15252/embr.201642450. Epub 2016 Jun 27.

Abstract

Receptor kinases convey diverse environmental and developmental inputs by sensing extracellular ligands. In plants, one group of receptor-like kinases (RLKs) is characterized by extracellular leucine-rich repeat (LRR) domains, which interact with various ligands that include the plant hormone brassinosteroid and peptides of the CLAVATA3/EMBRYO SURROUNDING REGION (CLE) type. For instance, the CLE45 peptide requires the LRR-RLK BARELY ANY MERISTEM 3 (BAM3) to prevent protophloem formation in Arabidopsis root meristems. Here, we show that other proposed CLE45 receptors, the two redundantly acting LRR-RLKs STERILITY-REGULATING KINASE MEMBER 1 (SKM1) and SKM2 (which perceive CLE45 in the context of pollen tube elongation), cannot substitute for BAM3 in the root. Moreover, we identify MEMBRANE-ASSOCIATED KINASE REGULATOR 5 (MAKR5) as a post-transcriptionally regulated amplifier of the CLE45 signal that acts downstream of BAM3. MAKR5 belongs to a small protein family whose prototypical member, BRI1 KINASE INHIBITOR 1, is an essentially negative regulator of brassinosteroid signaling. By contrast, MAKR5 is a positive effector of CLE45 signaling, revealing an unexpected diversity in the conceptual roles of MAKR genes in different signaling pathways.

Keywords: CLE peptide; SKM1; SKM2; protophloem; receptor‐like kinase.

MeSH terms

  • Arabidopsis / genetics*
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / genetics*
  • Arabidopsis Proteins / metabolism*
  • Gene Expression Regulation, Plant
  • Membrane Proteins / metabolism*
  • Phenotype
  • Plant Roots / genetics
  • Plant Roots / metabolism
  • Protein Serine-Threonine Kinases / metabolism*
  • Signal Transduction*
  • Transcription, Genetic

Substances

  • Arabidopsis Proteins
  • CLE45 protein, Arabidopsis
  • Membrane Proteins
  • BAM3 protein, Arabidopsis
  • Protein Serine-Threonine Kinases