Roles of the Two Drosophila CRYPTOCHROME Structural Domains in Circadian Photoreception

@article{Busza2004RolesOT,
  title={Roles of the Two Drosophila CRYPTOCHROME Structural Domains in Circadian Photoreception},
  author={Ania Busza and Myai Emery-Le and Michael Rosbash and Patrick Emery},
  journal={Science},
  year={2004},
  volume={304},
  pages={1503 - 1506}
}
CRYPTOCHROME (CRY) is the primary circadian photoreceptor in Drosophila. We show that CRY binding to TIMELESS (TIM) is light-dependent in flies and irreversibly commits TIM to proteasomal degradation. In contrast, CRY degradation is dependent on continuous light exposure, indicating that the CRY-TIM interaction is transient. A novel cry mutation (crym) reveals that CRY's photolyase homology domain is sufficient for light detection and phototransduction, whereas the carboxyl-terminal domain… Expand
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TLDR
The results indicate a role for CRY in circadian temperature as well as light regulation and suggest that these two features of the external 24-h cycle normally act together to dictate circadian phase. Expand
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TLDR
The current understanding of the mechanisms underlying CRY’s various circadian and noncircadian functions in fruit flies is reviewed. Expand
Cryptochrome Is a Regulator of Synaptic Plasticity in the Visual System of Drosophila melanogaster
TLDR
Evidence is presented that light-activated CRY may decrease BRP levels in photoreceptor termini in the distal lamina, probably targeting BRP for degradation, and that CRY-BRP complexes are located mainly in the visual system. Expand
Structure and function of animal cryptochromes.
TLDR
Animal CRYs have DNA-binding and autokinase activities, and their flavin cofactor is reduced by photoinduced electron transfer, and in mammals, the two CRY proteins are core components of the molecular clock and potential circadian photoreceptors. Expand
Flavin reduction activates Drosophila cryptochrome
TLDR
This study supports a model for CRY signaling in which flavin reduction is the critical step performed by light, and shows that reduction of the flavin to the anionic semiquinone by light or chemicals releases the CTT to activate dCRY. Expand
Structure of Full-length Drosophila Cryptochrome
TLDR
A 2.3-Å resolution crystal structure of Drosophila CRY with an intact C terminus is reported, demonstrating how conserved protein architecture and photochemistry can be elaborated into a range of light-driven functions. Expand
One Actor, Multiple Roles: The Performances of Cryptochrome in Drosophila
TLDR
Drosophila melanogaster possesses just one CRY, belonging to type 1 CRYs, but this single CRY appears to have different functions, specific to different organs, tissues, and even subset of cells in which it is expressed. Expand
Drosophila CRYPTOCHROME Is a Circadian Transcriptional Repressor
TLDR
Drosophila CRY functions as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells. Expand
Reaction mechanism of Drosophila cryptochrome
TLDR
It is found that exposure of CRY to blue light induces a conformation similar to that of the constitutively active CRY mutant with a C-terminal deletion (CRYΔ), which leads to a plausible model for circadian photoreception/phototransduction in Drosophila. Expand
The cryptochromes
SummaryCryptochromes are photoreceptors that regulate entrainment by light of the circadian clock in plants and animals. They also act as integral parts of the central circadian oscillator in animalExpand
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References

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TLDR
CRYPTOCHROME (CRY), a protein involved in circadian photoperception in Drosophila, is shown to block the function of PERIOD/TIMELESS (PER/Tim) heterodimeric complexes in a light-dependent fashion. Expand
Photic Signaling by Cryptochrome in the DrosophilaCircadian System
TLDR
This work dissected the early events in photic resetting by determining the mechanisms underlying the CRY response to light and by investigating the relationship between CRY and the light-induced ubiquitination of the TIM protein. Expand
CRY, a Drosophila Clock and Light-Regulated Cryptochrome, Is a Major Contributor to Circadian Rhythm Resetting and Photosensitivity
TLDR
It is proposed that CRY is a major Drosophila photoreceptor dedicated to the resetting of circadian rhythms, and physiological and genetic data link a specific photorecept molecule to circadian rhythmicity. Expand
The cryb Mutation Identifies Cryptochrome as a Circadian Photoreceptor in Drosophila
TLDR
Cryb flies are rhythmic in constant darkness, correlating with robust PER and TIM cycling in certain pacemaker neurons, and is an apparent null mutation in a gene encoding Drosophila's version of the blue light receptor cryptochrome. Expand
Drosophila cryptochromes: A unique circadian-rhythm photoreceptor
TLDR
It is shown that a mutation in a cryptochrome from the fruitfly Drosophila blocks an essential photoresponse of circadian rhythms, namely arrhythmicity under constant light conditions, and that there is probably no other comparable photoreceptor in this species. Expand
A new role for cryptochrome in a Drosophila circadian oscillator
TLDR
It is shown that CRY contributes to oscillator function and physiological output rhythms in the antenna during and after entrainment to light–dark cycles and after photic input is eliminated by entraining flies to temperature cycles, indicating fundamental differences between central and peripheral oscillator mechanisms in Drosophila. Expand
Drosophila CRY Is a Deep Brain Circadian Photoreceptor
TLDR
CRY overexpression in brain pacemaker cells increases behavioral photosensitivity, and this restricted CRY expression also rescues all circadian defects of cry(b) behavior. Expand
Circadian Photoreception in Drosophila: Functions of Cryptochrome in Peripheral and Central Clocks
TLDR
It is concluded that cryptochrome is involved in TIM-mediated entrainment of both central LN and peripheral MT clocks, and that neural and epithelial cells share the core clock mechanism, some clock components and light-entrainment pathways appear to have tissue-specific roles. Expand
The C Termini of Arabidopsis Cryptochromes Mediate a Constitutive Light Response
TLDR
It is proposed that the C-terminal domain of Arabidopsis cryptochrome is maintained in an inactive state in the dark through an intra- or intermolecular redox reaction mediated through the flavin bound to the N- terminus of the photolyase-like domain. Expand
Cryptochromes Enabling Plants and Animals to Determine Circadian Time
Cryptochromes are flavin-containing blue light photoreceptors related to photolyases-they are found in both plants and animals and have recently been described for bacteria. In plants, cryptochromesExpand
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