Structural and functional insights into core ABA signaling

Curr Opin Plant Biol. 2010 Oct;13(5):495-502. doi: 10.1016/j.pbi.2010.09.007. Epub 2010 Oct 9.

Abstract

A series of papers in the last year reported major advances in our understanding of abscisic acid (ABA) signaling: the identification of soluble ABA receptors, the elucidation of a core ABA signaling pathway and structural insights into the mechanism of ABA perception and signaling. Here we summarize these advances, which have shown in atomic resolution that the ABA receptors PYR1, PYL1 and PYL2 function as allosteric switches that inhibit type 2C protein phosphatases (PP2Cs) in response to ABA. These receptors function at the apex of a core signaling pathway that regulates ABA responses by controlling SnRK2 kinase activity and the phosphorylation of downstream target proteins such as ABFs, which control nuclear responses, and the ion channel SLAC1, which mediates electrophysiological responses to ABA.

Publication types

  • Review

MeSH terms

  • Abscisic Acid / physiology*
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / metabolism
  • Gene Expression Regulation, Plant
  • Membrane Proteins / metabolism
  • Membrane Transport Proteins / metabolism
  • Phosphoprotein Phosphatases / metabolism
  • Phosphorylation
  • Protein Phosphatase 2C
  • Protein Serine-Threonine Kinases / metabolism
  • Signal Transduction*

Substances

  • Arabidopsis Proteins
  • Membrane Proteins
  • Membrane Transport Proteins
  • Pyr1 protein, Arabidopsis
  • SLAC1 protein, Arabidopsis
  • SnRK2 protein, Arabidopsis
  • Abscisic Acid
  • Protein Serine-Threonine Kinases
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 2C