Casein kinase Iɛ in the Wnt pathway: Regulation of β-catenin function

Sakanaka, Chie; Leong, P. C.; Xu, Licen; Harrison, S.C.; Williams, Lewis T.

doi:10.1073/pnas.96.22.12548

Cited by 203 publications

(206 citation statements)

References 28 publications

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“…It has long been known that CK1 isoforms play crucial roles in the Wnt/β‐catenin signalling 28, 29, 30, 34, 35, 43, 44, 45, 46. In fact, early observations that overexpression of CK1 isoforms in Xenopus embryos caused axis duplication suggested a positive role for CK1 in Wnt signalling 47.…”

Section: Discussionmentioning

confidence: 99%

PAWS 1 controls Wnt signalling through association with casein kinase 1α

Bozatzi

Dingwell

et al. 2018

EMBO Reports

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The BMP and Wnt signalling pathways determine axis specification during embryonic development. Our previous work has shown that PAWS1 (also known as FAM83G) interacts with SMAD1 and modulates BMP signalling. Here, surprisingly, we show that overexpression of PAWS1 in Xenopus embryos activates Wnt signalling and causes complete axis duplication. Consistent with these observations in Xenopus, Wnt signalling is diminished in U2OS osteosarcoma cells lacking PAWS1, while BMP signalling is unaffected. We show that PAWS1 interacts and co‐localises with the α isoform of casein kinase 1 (CK1), and that PAWS1 mutations incapable of binding CK1 fail both to activate Wnt signalling and to elicit axis duplication in Xenopus embryos.

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Section: Discussionmentioning

confidence: 99%

PAWS 1 controls Wnt signalling through association with casein kinase 1α

Bozatzi

Dingwell

et al. 2018

EMBO Reports

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“…Other upregulated genes in secondary hair follicles include fibroblast growth factor 21 (GOAT_ENSP00000222157), which can promote the transition to catagen 37 , and casein kinase Iε(goat_ GLEAN_10015556), an important regulator of β-catenin in the Wnt pathway, which is one of the most important pathways in hair follicle development 38 .…”

Section: A R T I C L E Smentioning

confidence: 99%

“…Other downregulated genes included Gap junction alpha-1 protein (goat_GLEAN_10013034) and Desmoglein 1 (GOAT_ENSBTAP00000018382), which have been reported to be involved in hair follicle cell communication and hair follicle morphogenesis 38,39 , and isopentenyl-diphosphate deltaisomerase 1 (GOAT_ENSBTAP00000005323) and cellular retinoic acid-binding protein 2 (GOAT_ENSBTAP00000007515), which are both related to retinoic acid biosynthesis and can regulate hair growth and the hair life cycle through Wnt signaling 40,41 . Further analyses of these expression data generated additional hypotheses related to genes and pathways that may underlie cashmere fiber production (Supplementary Discussion, Supplementary Fig.…”

Section: A R T I C L E Smentioning

confidence: 99%

Sequencing and automated whole-genome optical mapping of the genome of a domestic goat (Capra hircus)

et al. 2012

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“…Our earlier observations were consistent with those for well-known MAPK pathway regulation through phosphorylation and dephosphorylation in eggs. It is known that casein kinase I epsilon regulates developmental and oncogenic processes as a positive regulator of the Wnt signalling pathway (33). The enzymatic activity of casein kinase I epsilon is known to be suppressed by autophosphorylation (34).…”

Section: Validation Of Phosphorylation Sitesmentioning

confidence: 99%

Exploring the phosphoproteome profiles duringXenopusegg activation by calcium stimulation using a fully automated phosphopeptide purification system

Kanno

Horigome

2015

J Biochem

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To explore the phosphoproteome profiles during Xenopus egg activation by Ca 2+ -stimulation, an automated phosphopeptide purification system involving a titania column was improved by introducing 4-step elution with phosphate buffers. The number of detected phosphopeptides in the tryptic digest of a Xenopus egg cytosol fraction on mass spectrometry (MS) was increased 1.5-fold and the percentage of multiply phosphorylated peptides increased from 17 to 24% with introduction of the 4-step elution method. Phosphopeptides were purified by the improved method from tryptic digests of cytosol fractions of Xenopus eggs without and with a Ca 2+ -stimulus, and then, analysed by MS. One thousand three hundred and seventy-five and 994 phosphopeptides were reproducibly detected on duplicate MS, respectively. They included 818 and 437 phosphopeptides specific to each digest, respectively. A method involving isobaric tags for relative and absolute quantitation (iTRAQ) was also applied to compare the phosphorylation levels in Xenopus eggs without and with a Ca 2+ -stimulus, the ratios for 112 phosphopeptides in tryptic digests of these egg cytosol fractions being obtained. It was suggested from all the results that the phosphorylation sites and levels change during Xenopus egg activation for many known and unknown sites on structural proteins, signalling related proteins, cell cyclerelated proteins and others.Keywords: egg/phosphoproteome/proteome/titania/ Xenopus.Abbreviations: 4EBP, eukaryotic translation initiation factor 4E binding protein; iTRAQ, isobaric tags for relative and absolute quantitation; LC MS/MS, nano-flow liquid chromatography-linear ion trap/ Orbitrap tandem mass spectrometry; MAPK, mitogen-activated protein kinase; MS, mass spectrometry; mTOR, mammalian target of rapamycin; m/z, massto-charge ratio; ODS, octadecylsilica; TFA, trifluoroacetic acid.Xenopus eggs have been used in studies on egg maturation, egg activation and other mechanisms, which facilitated the progress of developmental biology (1, 2). It has been shown that signalling pathways including protein phosphorylation and dephosphorylation participate greatly in these regulation mechanisms (1, 3, 4). To clarify the complicated regulation mechanism of egg activation, comprehensive analysis of protein phosphorylation during egg activation is a powerful means. The cell cycle of Xenopus eggs is arrested at the second meiotic metaphase. So, Xenopus eggs without Ca 2+ -stimulation show meiotic metaphase properties. When eggs are activated by Ca 2+ -stimulation to mimic fertilization, they show synthetic phase properties. So, we can analyse the changes of protein phosphorylation during activation of Xenopus eggs by comparison of the phosphorylation in Ca 2+ -unstimulated and Ca 2+ -stimulated eggs (5). In this study, therefore, we obtained phosphoproteome profiles of Xenopus egg cytosol fractions without and with Ca 2+ -stimulation as a basis for understanding the egg activation mechanism.To obtain high quality phosphoproteome data, i) determination of a ...

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Casein kinase Iɛ in the Wnt pathway: Regulation of β-catenin function

Abstract: Wnt and its intracellular effector

Cited by 203 publications

References 28 publications

PAWS 1 controls Wnt signalling through association with casein kinase 1α

PAWS 1 controls Wnt signalling through association with casein kinase 1α

Sequencing and automated whole-genome optical mapping of the genome of a domestic goat (Capra hircus)

Exploring the phosphoproteome profiles duringXenopusegg activation by calcium stimulation using a fully automated phosphopeptide purification system

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