John Klejnot

TL;DR: The identification and characterization of the Arabidopsis CIB1 (cryptochrome-interacting basic-helix-loop-Helix) protein is reported, and it is proposed that the blue light–dependent interaction of cryptochrome(s) with C IB1 and CIB 1-related proteins represents an early photoreceptor signaling mechanism in plants.

TL;DR: It is hypothesized that photons excite electrons of the flavin molecule, resulting in redox reaction or circular electron shuttle and conformational changes of the photoreceptors, which alters gene expression at both transcriptional and posttranslational levels and consequently the metabolic and developmental programs of plants.

TL;DR: The results show that CRY2 mediates blue light inhibition of hypocotyl elongation and photoperiodic promotion of floral initiation in the nucleus, and it is demonstrated that a photoreceptor can complete its posttranslational life cycle inside the nucleus.

TL;DR: It was found that CRY2-GFP, but not GFP-CRY2, formed distinct nuclear bodies in response to blue light, suggesting that the nuclear bodies may result from accumulation of photoexcited CRy2- GFP waiting to be degraded.

TL;DR: The results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2, and it was proposed that the PHR domain and the C-terminal tail of the unphosphorylatedCRY2 form a “closed” conformation to suppress the NC80 motif in the absence of light.