A Role for Casein Kinase 2 in the Mechanism Underlying Circadian Temperature Compensation

被引：100

作者：

Mehra, Arun ^{[1
]}

Shi, Mi ^{[1
]}

Baker, Christopher L. ^{[1
]}

Colot, Hildur V. ^{[1
]}

Loros, Jennifer J. ^{[1
,2
]}

Dunlap, Jay C. ^{[1
,2
]}

机构：

[1] Dartmouth Coll, Hitchcock Med Ctr, Dartmouth Med Sch, Dept Genet, Hanover, NH 03755 USA

[2] Dartmouth Coll, Hitchcock Med Ctr, Dartmouth Med Sch, Dept Biochem, Hanover, NH 03755 USA

来源：

CELL | 2009年 / 137卷 / 04期

基金：

美国国家卫生研究院; 加拿大健康研究院;

关键词：

PERIOD LENGTH; FREQUENCY DETERMINES; NEUROSPORA CLOCK; PROTEIN; PHOSPHORYLATION; DROSOPHILA; RHYTHMS; GENE; TIME; CK2;

D O I：

10.1016/j.cell.2009.03.019

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：749 / 760

页数：12

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