Structure and function of the UV-B photoreceptor UVR8

Curr Opin Struct Biol. 2014 Dec:29:52-7. doi: 10.1016/j.sbi.2014.09.004. Epub 2014 Oct 7.

Abstract

UVR8 is a UV-B photoreceptor that employs specific tryptophans in its primary sequence as chromophores in photoreception. UV-B absorption causes dissociation of the dimeric photoreceptor by neutralizing interactions between monomers. The monomeric form initiates signalling through interaction with the COP1 protein, leading to transcriptional responses. This article discusses the structural basis of UVR8 function, highlighting recent research on the mechanism of photoreception and on interactions with other proteins involved in signalling and regulation.

Publication types

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

MeSH terms

  • Arabidopsis / chemistry*
  • Arabidopsis Proteins / chemistry*
  • Chromosomal Proteins, Non-Histone / chemistry*
  • Models, Molecular
  • Photoreceptors, Plant / chemistry*
  • Protein Conformation
  • Protein Multimerization
  • Signal Transduction
  • Ubiquitin-Protein Ligases / chemistry

Substances

  • Arabidopsis Proteins
  • Chromosomal Proteins, Non-Histone
  • Photoreceptors, Plant
  • Uvr8 protein, Arabidopsis
  • AT2G32950 protein, Arabidopsis
  • Ubiquitin-Protein Ligases