Roles of the two Drosophila CRYPTOCHROME structural domains in circadian photoreception

UMMS Affiliation

Department of Neurobiology; Emery Lab; Graduate School of Biomedical Sciences, MD/PhD Program; Graduate School of Biomedical Sciences, Neuroscience Program

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Document Type



Animals; Animals, Genetically Modified; Cell Line; *Circadian Rhythm; Cysteine Endopeptidases; Darkness; Drosophila Proteins; Drosophila melanogaster; Eye Proteins; Female; *Light; Male; Multienzyme Complexes; Mutation; Nuclear Proteins; Photoreceptors, Invertebrate; Phototransduction; Proteasome Endopeptidase Complex; Protein Binding; Protein Structure, Tertiary; Receptors, G-Protein-Coupled


Neuroscience and Neurobiology


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 (cry(m)) reveals that CRY's photolyase homology domain is sufficient for light detection and phototransduction, whereas the carboxyl-terminal domain regulates CRY stability, CRY-TIM interaction, and circadian photosensitivity. This contrasts with the function of Arabidopsis CRY domains and demonstrates that insect and plant cryptochromes use different mechanisms.

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Citation: Science. 2004 Jun 4;304(5676):1503-6. Link to article on publisher's site

DOI of Published Version



Co-author Ania Busza is a student in the Neuroscience and MD/PhD programs in the Graduate School of Biomedical Sciences (GSBS) at UMass Medical School.

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Link to Article in PubMed

Journal/Book/Conference Title

Science (New York, N.Y.)

PubMed ID