SCAR mediates light-induced root elongation in Arabidopsis through photoreceptors and proteasomes

Plant Cell. 2011 Oct;23(10):3610-26. doi: 10.1105/tpc.111.088823. Epub 2011 Oct 4.

Abstract

The ARP2/3 complex, a highly conserved nucleator of F-actin, and its activator, the SCAR complex, are essential for growth in plants and animals. In this article, we present a pathway through which roots of Arabidopsis thaliana directly perceive light to promote their elongation. The ARP2/3-SCAR complex and the maintenance of longitudinally aligned F-actin arrays are crucial components of this pathway. The involvement of the ARP2/3-SCAR complex in light-regulated root growth is supported by our finding that mutants of the SCAR complex subunit BRK1/HSPC300, or other individual subunits of the ARP2/3-SCAR complex, showed a dramatic inhibition of root elongation in the light, which mirrored reduced growth of wild-type roots in the dark. SCAR1 degradation in dark-grown wild-type roots by constitutive photomorphogenic 1 (COP1) E3 ligase and 26S proteasome accompanied the loss of longitudinal F-actin and reduced root growth. Light perceived by the root photoreceptors, cryptochrome and phytochrome, suppressed COP1-mediated SCAR1 degradation. Taken together, our data provide a biochemical explanation for light-induced promotion of root elongation by the ARP2/3-SCAR complex.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Actin-Related Protein 2-3 Complex / genetics
  • Actin-Related Protein 2-3 Complex / metabolism*
  • Actins / metabolism
  • Arabidopsis / genetics
  • Arabidopsis / physiology*
  • Arabidopsis / radiation effects
  • Arabidopsis / ultrastructure
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Cysteine Proteinase Inhibitors / pharmacology
  • Darkness
  • Leupeptins / pharmacology
  • Light
  • Light Signal Transduction / physiology
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Mutation
  • Phenotype
  • Photoreceptors, Plant / genetics
  • Photoreceptors, Plant / metabolism*
  • Phytochrome / genetics
  • Phytochrome / metabolism
  • Plant Components, Aerial / genetics
  • Plant Components, Aerial / physiology
  • Plant Components, Aerial / radiation effects
  • Plant Components, Aerial / ultrastructure
  • Plant Roots / genetics
  • Plant Roots / physiology*
  • Plant Roots / radiation effects
  • Plant Roots / ultrastructure
  • Plants, Genetically Modified
  • Proteasome Endopeptidase Complex / genetics
  • Proteasome Endopeptidase Complex / metabolism*
  • Proteasome Inhibitors
  • Protein Binding
  • Seedlings / genetics
  • Seedlings / physiology
  • Seedlings / radiation effects
  • Seedlings / ultrastructure
  • Ubiquitin-Protein Ligases / genetics
  • Ubiquitin-Protein Ligases / metabolism

Substances

  • Actin-Related Protein 2-3 Complex
  • Actins
  • Arabidopsis Proteins
  • Cysteine Proteinase Inhibitors
  • Leupeptins
  • Microfilament Proteins
  • Photoreceptors, Plant
  • Proteasome Inhibitors
  • SCAR1 protein, Arabidopsis
  • Phytochrome
  • AT2G32950 protein, Arabidopsis
  • Ubiquitin-Protein Ligases
  • Proteasome Endopeptidase Complex
  • ATP dependent 26S protease
  • benzyloxycarbonylleucyl-leucyl-leucine aldehyde