Crystallographic studies of casein kinase I δ: toward a structural understanding of auto-inhibition

Longenecker, K.L.; Roach, Peter J.; Hurley, Thomas D.

doi:10.1107/s0907444997011724

Cited by 32 publications

(29 citation statements)

References 18 publications

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“…All members share a near-consensus SV40 T antigen putative nuclear localization signal (NLS). An anion-binding site, which is formed by three residues conserved throughout the CKI family (88)(89)(90), recognizes the phosphate ester of the substrate. The CKI family has broad substrate specificity and ubiquitous subcellular localization (85).…”

Section: Discussionmentioning

confidence: 99%

Positional Syntenic Cloning and Functional Characterization of the Mammalian Circadian Mutation tau

Lowrey¹,

Shimomura

Antoch

et al. 2000

Science

802

594

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The tau mutation is a semidominant autosomal allele that dramatically shortens period length of circadian rhythms in Syrian hamsters. We report the molecular identification of the tau locus using genetically directed representational difference analysis to define a region of conserved synteny in hamsters with both the mouse and human genomes. The tau locus is encoded by casein kinase I epsilon (CKIɛ), a homolog of the Drosophila circadian gene double-time. In vitro expression and functional studies of wild-type and tau mutant CKIɛ enzyme reveal that the mutant enzyme has a markedly reduced maximal velocity and autophosphorylation state. In addition, in vitro CKIɛ can interact with mammalian PERIOD proteins, and the mutant enzyme is deficient in its ability to phosphorylate PERIOD. We conclude that tau is an allele of hamster CKIɛ and propose a mechanism by which the mutation leads to the observed aberrant circadian phenotype in mutant animals.Daily rhythms in biochemical, physiological, and behavioral processes are regulated by biological clocks (1, 2). In natural conditions, the endogenous circadian rhythms that are generated by these clocks are synchronized (entrained) to the 24-hour cycles of the external world by time cues such as the daily light/dark cycle (2). While these clocks are found in organisms as divergent as cyanobacteria, plants, fruit flies, and mammals, there is an extraordinary degree of evolutionary conservation of the underlying generative molecular mechanisms (3-9). The first mammalian circadian gene, Clock, was cloned and characterized in mouse (10-12). Clock encodes a novel member of the basic helix-loop-helix (bHLH) PER-ARNT-SIM (PAS) family of transcription factors. Shortly following the cloning of Clock, three mouse Period orthologs, denoted mPer1 (13,14), and mPer3 (18, 19), as well as a Timeless (mTim) ortholog, were cloned (20)(21)(22)(23)(24). At the same time, another gene, BMAL1 (25), was found to encode the protein dimerization partner for CLOCK (26), and together the CLOCK/BMAL complex was shown to transactivate mPer1 via conserved E-box elements found in the promoters of Drosophila and mouse period genes (26-28). Finally, in Drosophila and mammals, the negative feedback effects of PER and TIM were shown to act at the level of the CLOCK/BMAL complex (20, 28) in a surprisingly direct manner (29, 30).

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Section: Discussionmentioning

confidence: 99%

Positional Syntenic Cloning and Functional Characterization of the Mammalian Circadian Mutation tau

Lowrey¹,

Shimomura

Antoch

et al. 2000

Science

802

594

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“…Despite its simple structure, CK1 is regulated in multiple ways, including inhibition by autophosphorylation, subcellular distribution, and probably also dimerization (Longenecker et al 1998). We wondered whether the Neurospora CK1a isoforms are differentially distributed and whether they interact with each other.…”

Section: Biochemical Properties Of Ck1amentioning

confidence: 99%

Posttranslational Regulation ofNeurosporaCircadian Clock by CK1a-dependent Phosphorylation

Querfurth¹,

Diernfellner²,

Heise³

et al. 2007

Cold Spring Harbor Symposia on Quantitative Biology

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“…5b). A similar dimer interface to that observed in P2 1 CK1 (1-299) was described for two molecules of CK1 (1-342) related to one another by a crystallographic twofold axis in a C222 1 crystal structure (coordinates not deposited; Longenecker et al, 1998). Although this is an extensive dimer interface that occurs in at least three different crystal forms, size-exclusion chromatography indicates that CK1 is a monomer in solution.…”

Section: Dimer Interface and Crystal Packingmentioning

confidence: 82%

A monoclinic crystal form of casein kinase 1 δ

et al. 2013

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PDB Reference: casein kinase 1 , 4jjrCasein kinase 1 (CK1) is a regulatory enzyme in the mammalian circadian oscillator and represents a potential pharmacological target for modulating circadian rhythms. Crystal structures of four different polymorphs of CK1 have previously been determined and this article reports the crystallization and structure determination of a new crystal form belonging to space group P2 1 . Comparison of CK1 crystal structures reveals few conformational differences within the C-terminal lobe, but more significant movements of the -sheet region of the N-terminal lobe were observed.

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Crystallographic studies of casein kinase I δ: toward a structural understanding of auto-inhibition

Cited by 32 publications

References 18 publications

Positional Syntenic Cloning and Functional Characterization of the Mammalian Circadian Mutation tau

Positional Syntenic Cloning and Functional Characterization of the Mammalian Circadian Mutation tau

Posttranslational Regulation ofNeurosporaCircadian Clock by CK1a-dependent Phosphorylation

A monoclinic crystal form of casein kinase 1 δ

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