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

Publication Date


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.

DOI of Published Version



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

Journal/Book/Conference Title

Science (New York, N.Y.)


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

PubMed ID