Recent advances in UV-B signalling: interaction of proteins with the UVR8 photoreceptor.

Abstract

The UV RESISTANCE LOCUS 8 (UVR8) photoreceptor mediates many plant responses to UV-B and short wavelength UV-A light. UVR8 functions through interactions with other proteins which lead to extensive changes in gene expression. Interactions with particular proteins determine the nature of the response to UV-B. It is therefore important to understand the molecular basis of these interactions: how are different proteins able to bind to UVR8 and how is differential binding regulated? This concise review highlights recent developments in addressing these questions. Key advances are discussed with regard to: identification of proteins that interact with UVR8; the mechanism of UVR8 accumulation in the nucleus; the photoactivation of UVR8 monomer; the structural basis of interaction between UVR8 and CONSTITUTIVELY PHOTOMORPHOGENIC 1 (COP1) and REPRESSOR OF UV-B PHOTOMORPHOGENESIS (RUP) proteins; and the role of UVR8 phosphorylation in modulating interactions and responses to UV-B. Nevertheless, much remains to be understood, and the need to extend future research to the growing list of interactors is emphasized.