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...

Full description

Saved in:
Bibliographic Details
Published inCell research Vol. 23; no. 12; pp. 1417 - 1419
Main Authors Nangle, Shannon, Xing, Weiman, Zheng, Ning
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.12.2013
Nature Publishing Group
Subjects
Online AccessGet full text
ISSN1001-0602
1748-7838
1748-7838
DOI10.1038/cr.2013.136

Cover

Loading…
More Information
Summary: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].
Bibliography: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.
ISSN:1001-0602
1748-7838
1748-7838
DOI:10.1038/cr.2013.136