Glycogen synthase kinase is a regulator of the circadian clock of Neurospora crassa

Timekeeping by circadian clocks relies upon precise adjustment of expression levels of clock proteins. Here we identify glycogen synthase kinase (GSK) as a novel and critical component of the circadian clock of Neurospora crassa that regulates the abundance of its core transcription factor white col...

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Bibliographic Details
Main Authors: Tataroglu, Ozgur (Author) , Lauinger, Linda (Author) , Sancar, Gencer (Author) , Brunner, Michael (Author) , Diernfellner, Axel (Author)
Format: Article (Journal)
Language:English
Published: September 6, 2012
In: The journal of biological chemistry
Year: 2012, Volume: 287, Issue: 44, Pages: 36936-36943
ISSN:1083-351X
DOI:10.1074/jbc.M112.396622
Online Access:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1074/jbc.M112.396622
Verlag, kostenfrei, Volltext: http://www.jbc.org/content/287/44/36936
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Author Notes:Özgür Tataroğlu, Linda Lauinger, Gencer Sancar, Katharina Jakob, Michael Brunner, and Axel C.R. Diernfellner
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Summary:Timekeeping by circadian clocks relies upon precise adjustment of expression levels of clock proteins. Here we identify glycogen synthase kinase (GSK) as a novel and critical component of the circadian clock of Neurospora crassa that regulates the abundance of its core transcription factor white collar complex (WCC) on a post-transcriptional level. We show that GSK specifically binds and phosphorylates both subunits of the WCC. Reduced expression of GSK promotes an increased accumulation of WC-1, the limiting factor of the WCC, causing an acceleration of the circadian clock and a shorter free-running period.
Item Description:Gesehen am 13.07.2018
Physical Description:Online Resource
ISSN:1083-351X
DOI:10.1074/jbc.M112.396622