Journal
CELL
Volume 137, Issue 4, Pages 749-760Publisher
CELL PRESS
DOI: 10.1016/j.cell.2009.03.019
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Funding
- Canadian Institutes of Health Research Postdoctoral Fellowship
- National Institutes of Health [R01 GM34985, P01 GM68087, R01 GM083336]
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Temperature compensation of circadian clocks is an unsolved problem with relevance to the general phenomenon of biological compensation. We identify casein kinase 2 (CK2) as a key regulator of temperature compensation of the Neurospora clock by determining that two long-standing clock mutants, chrono and period-3, displaying distinctive alterations in compensation encode the beta 1 and alpha subunits of CK2, respectively. Reducing the dose of these subunits, particularly beta 1, significantly alters temperature compensation without altering the enzyme's Q(10). By contrast, other kinases and phosphatases implicated in clock function do not play appreciable roles in temperature compensation. CK2 exerts its effects on the clock by directly phosphorylating FREQUENCY (FRQ), and this phosphorylation is compromised in CK2 hypomorphs. Finally, mutation of certain putative CK2 phosphosites on FRQ, shown to be phosphorylated in vivo, predictably alters temperature compensation profiles effectively phenocopying CK2 mutants.
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