Crystal structure of mammalian cryptochrome in complex with a small molecule competitor of its ubiquitin ligase
Dear Editor, The cryptochrome （CRY） flavoproteins are criti cal components of the mammalian molecular circa dian clock, which operates through an auto-regulatory transcription-translation feedback loop [1]. In this clockwork, a pair of transcription factors, CLOCK and BMAL1, drive the expression of...
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| Published in | Cell research Vol. 23; no. 12; pp. 1417 - 1419 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
01.12.2013
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1001-0602 1748-7838 1748-7838 |
| DOI | 10.1038/cr.2013.136 |
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| Abstract | Dear Editor, The cryptochrome （CRY） flavoproteins are criti cal components of the mammalian molecular circa dian clock, which operates through an auto-regulatory transcription-translation feedback loop [1]. In this clockwork, a pair of transcription factors, CLOCK and BMAL1, drive the expression of CRYs, Periods （PERs）, and other clock-controlled genes, while CRYs and PERs heterodimerize and repress their own gene expression by inhibiting CLOCK-BMALl-mediated transcription [2, 3]. To establish rhythmic protein oscillation, CRYs are ubiq- uitinated by the SCF^FBXL3 ubiquitin ligase and targeted for rapid proteasomal degradation [4-6]. |
|---|---|
| AbstractList | Dear Editor, The cryptochrome （CRY） flavoproteins are criti cal components of the mammalian molecular circa dian clock, which operates through an auto-regulatory transcription-translation feedback loop [1]. In this clockwork, a pair of transcription factors, CLOCK and BMAL1, drive the expression of CRYs, Periods （PERs）, and other clock-controlled genes, while CRYs and PERs heterodimerize and repress their own gene expression by inhibiting CLOCK-BMALl-mediated transcription [2, 3]. To establish rhythmic protein oscillation, CRYs are ubiq- uitinated by the SCF^FBXL3 ubiquitin ligase and targeted for rapid proteasomal degradation [4-6]. |
| Author | Zheng, Ning Nangle, Shannon Xing, Weiman |
| Author_xml | – sequence: 1 givenname: Shannon surname: Nangle fullname: Nangle, Shannon organization: Department of Pharmacology, University of Washington – sequence: 2 givenname: Weiman surname: Xing fullname: Xing, Weiman email: wxing@uw.edu organization: Department of Pharmacology, University of Washington, Howard Hughes Medical Institute, Box 357280, University of Washington – sequence: 3 givenname: Ning surname: Zheng fullname: Zheng, Ning email: nzheng@uw.edu organization: Department of Pharmacology, University of Washington, Howard Hughes Medical Institute, Box 357280, University of Washington |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24080726$$D View this record in MEDLINE/PubMed |
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| Notes | 31-1568/Q Dear Editor, The cryptochrome （CRY） flavoproteins are criti cal components of the mammalian molecular circa dian clock, which operates through an auto-regulatory transcription-translation feedback loop [1]. In this clockwork, a pair of transcription factors, CLOCK and BMAL1, drive the expression of CRYs, Periods （PERs）, and other clock-controlled genes, while CRYs and PERs heterodimerize and repress their own gene expression by inhibiting CLOCK-BMALl-mediated transcription [2, 3]. To establish rhythmic protein oscillation, CRYs are ubiq- uitinated by the SCF^FBXL3 ubiquitin ligase and targeted for rapid proteasomal degradation [4-6]. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Correspondence-3 ObjectType-Article-2 ObjectType-Correspondence-1 content type line 23 These two authors contributed equally to this work. |
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| SubjectTerms | 631/45/612/1225 631/535 631/80/474/2073 Animals Binding Sites Biomedical and Life Sciences Carbazoles - chemistry Carbazoles - metabolism Cell Biology Cryptochromes - chemistry Cryptochromes - metabolism Crystallography, X-Ray F-Box Proteins - chemistry F-Box Proteins - metabolism Flavin-Adenine Dinucleotide - chemistry Flavin-Adenine Dinucleotide - metabolism Letter to the Editor Life Sciences Mice Models, Molecular Protein Binding Protein Structure, Tertiary Sulfonamides - chemistry Sulfonamides - metabolism Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - metabolism 哺乳动物 小分子 晶体结构 泛素连接酶 竞争 转录因子 隐花色素 黄素蛋白 |
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| Title | Crystal structure of mammalian cryptochrome in complex with a small molecule competitor of its ubiquitin ligase |
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