Title

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

6-5-2004

Document Type

Article

Subjects

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

Disciplines

Neuroscience and Neurobiology

Abstract

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.

Rights and Permissions

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

DOI of Published Version

10.1126/science.1096973

Comments

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.

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

Science (New York, N.Y.)

PubMed ID

15178801