Show simple item record

Roles of the two Drosophila CRYPTOCHROME structural domains in circadian photoreception

dc.contributor.authorBusza, Ania
dc.contributor.authorEmery-Le, Myai
dc.contributor.authorRosbash, Michael
dc.contributor.authorEmery, Patrick
dc.date2022-08-11T08:09:35.000
dc.date.accessioned2022-08-23T16:36:26Z
dc.date.available2022-08-23T16:36:26Z
dc.date.issued2004-06-05
dc.date.submitted2009-03-31
dc.identifier.citationScience. 2004 Jun 4;304(5676):1503-6. <a href="http://dx.doi.org/10.1126/science.1096973">Link to article on publisher's site</a>
dc.identifier.issn1095-9203 (Electronic)
dc.identifier.doi10.1126/science.1096973
dc.identifier.pmid15178801
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38788
dc.description<p>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.</p>
dc.description.abstractCRYPTOCHROME (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.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=15178801&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1126/science.1096973
dc.subjectAnimals
dc.subjectAnimals, Genetically Modified
dc.subjectCell Line
dc.subject*Circadian Rhythm
dc.subjectCysteine Endopeptidases
dc.subjectDarkness
dc.subjectDrosophila Proteins
dc.subjectDrosophila melanogaster
dc.subjectEye Proteins
dc.subjectFemale
dc.subject*Light
dc.subjectMale
dc.subjectMultienzyme Complexes
dc.subjectMutation
dc.subjectNuclear Proteins
dc.subjectPhotoreceptors, Invertebrate
dc.subjectPhototransduction
dc.subjectProteasome Endopeptidase Complex
dc.subjectProtein Binding
dc.subjectProtein Structure, Tertiary
dc.subjectReceptors, G-Protein-Coupled
dc.subjectNeuroscience and Neurobiology
dc.titleRoles of the two Drosophila CRYPTOCHROME structural domains in circadian photoreception
dc.typeJournal Article
dc.source.journaltitleScience (New York, N.Y.)
dc.source.volume304
dc.source.issue5676
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1633
dc.identifier.contextkey805454
html.description.abstract<p>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.</p>
dc.identifier.submissionpathoapubs/1633
dc.contributor.departmentGraduate School of Biomedical Sciences, Neuroscience Program
dc.contributor.departmentGraduate School of Biomedical Sciences, MD/PhD Program
dc.contributor.departmentEmery Lab
dc.contributor.departmentNeurobiology
dc.source.pages1503-6


This item appears in the following Collection(s)

Show simple item record