Turning off the blue-light response: In plants, blue light is perceived by cryptochromes, which, once activated, set off signaling events that regulate gene expression, circadian rhythms, and photomorphogenesis. Wang et al. now show that in the model plant Arabidopsis , one of the functions of activated cryptochromes, which are dimers or oligomers when active, is to activate production of the protein BIC1 (blue-light inhibitor of cryptochromes 1) (see the Perspective by Fankhauser and Ulm). BIC1 then favors monomerization and thus inactivation of the cryptochromes. This feedback loop resets the system so that blue-light responses can be turned off as well as turned on. Science , this issue p. 343 ; see also p. 282

Blue light affects many aspects of plant growth and development throughout the plant lifecycle. Plant cryptochromes (CRYs) are UV‐A/blue light photoreceptors that play pivotal roles in regulating blue light‐mediated physiological responses via the regulated expression of more than one thousand genes. Photoactivated CRYs regulate transcription via two distinct mechanisms: indirect promotion of the activity of transcription factors by inactivation of the COP1/SPA E3 ligase complex or direct activation or inactivation of at least two sets of basic helix–loop–helix transcription factor families by physical interaction. Hence, CRYs govern intricate mechanisms that modulate activities of transcription factors to regulate multiple aspects of blue light‐responsive photomorphogenesis. Here, we review recent progress in dissecting the pathways of CRY signaling and discuss accumulating evidence that shows how CRYs regulate broad physiological responses to blue light.

Plant cryptochromes undergo blue light-dependent phosphorylation to regulate their activity and abundance, but the protein kinases that phosphorylate plant cryptochromes have remained unclear. Here we show that photoexcited Arabidopsis cryptochrome 2 (CRY2) is phosphorylated in vivo on as many as 24 different residues, including 7 major phosphoserines. We demonstrate that four closely related Photoregulatory Protein Kinases (previously referred to as MUT9-like kinases) interact with and phosphorylate photoexcited CRY2. Analyses of the ppk123 and ppk124 triple mutants and amiR^4k artificial microRNA-expressing lines demonstrate that PPKs catalyse blue light-dependent CRY2 phosphorylation to both activate and destabilize the photoreceptor. Phenotypic analyses of these mutant lines indicate that PPKs may have additional substrates, including those involved in the phytochrome signal transduction pathway. These results reveal a mechanism underlying the co-action of cryptochromes and phytochromes to coordinate plant growth and development in response to different wavelengths of solar radiation in nature.

In nature, plants integrate a wide range of light signals from solar radiation to adapt to the surrounding light environment, and these light signals also regulate a variety of important agronomic traits. Blue light-sensing cryptochrome (cry) and red/far-red light-sensing phytochrome (phy) play critical roles in regulating light-mediated physiological responses via the regulated transcriptional network. Accumulating evidence in the model plant Arabidopsis has revealed that crys and phys share two mechanistically distinct pathways to coordinately regulate transcriptional changes in response to light. First, crys and phys promote the accumulation of transcription factors that regulate photomorphogenesis, such as HY5 and HFR1, via the inactivation of the CONSTITUTIVE PHOTOMORPHOGENIC1/SUPPRESSOR OF PHYA-105 E3 ligase complex by light-dependent binding. Second, photoactive crys and phys directly interact with PHYTOCHROME INTERACTING FACTOR transcription factor family proteins to regulate transcriptional activity. The coordinated regulation of these two pathways (and others) by crys and phys allow plants to respond with plasticity to fluctuating light environments in nature.