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Circadian conformational change of the Neurospora clock protein FREQUENCY triggered by clustered hyperphosphorylation of a basic domain

In the course of a day, the Neurospora clock protein FREQUENCY (FRQ) is progressively phosphorylated at up to 113 sites and eventually degraded. Phosphorylation and degradation are crucial for circadian time keeping, but it is not known how phosphorylation of a large number of sites correlates with...

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Bibliographic Details
Main Authors: Querfurth, Christina (Author) , Diernfellner, Axel (Author) , Gin, Elan (Author) , Malzahn, Erik (Author) , Höfer, Thomas (Author) , Brunner, Michael (Author)
Format: Article (Journal)
Language:English
Published: 1 September 2011
In: Molecular cell
Year: 2011, Volume: 43, Issue: 5, Pages: 713-722
ISSN:1097-4164
DOI:10.1016/j.molcel.2011.06.033
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.molcel.2011.06.033
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Author Notes:Christina Querfurth, Axel C.R. Diernfellner, Elan Gin, Erik Malzahn, Thomas Höfer, Michael Brunner
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Summary:In the course of a day, the Neurospora clock protein FREQUENCY (FRQ) is progressively phosphorylated at up to 113 sites and eventually degraded. Phosphorylation and degradation are crucial for circadian time keeping, but it is not known how phosphorylation of a large number of sites correlates with circadian degradation of FRQ. We show that two amphipathic motifs in FRQ interact over a long distance, bringing the positively charged N-terminal portion in spatial proximity to the negatively charged middle and C-terminal portion of FRQ. The interaction is essential for the recruitment of casein kinase 1a (CK1a) into a stable complex with FRQ. FRQ-bound CK1a progressively phosphorylates the positively charged N-terminal domain of FRQ at up to 46 nonconsensus sites, triggering a conformational change, presumably by electrostatic repulsion, that commits the protein for degradation via the PEST1 signal in the negatively charged central portion of FRQ.
Item Description:Gesehen am 23.01.2023
Physical Description:Online Resource
ISSN:1097-4164
DOI:10.1016/j.molcel.2011.06.033

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