Genomes and Genes
Gene Symbol: TPTEP2-CSNK1E
Description: TPTEP2-CSNK1E readthrough
Alias: LOC400927-CSNK1E, casein kinase I isoform epsilon, CKI-epsilon, LOC400927-CSNK1E readthrough
- Lee K, Johmura Y, Yu L, Park J, Gao Y, Bang J, et al. Identification of a novel Wnt5a-CK1?-Dvl2-Plk1-mediated primary cilia disassembly pathway. EMBO J. 2012;31:3104-17 pubmed publisher..This study may provide new insights into the mechanism underlying ciliary disassembly processes and various cilia-related disorders. ..
- McKenzie J, Riento K, Ridley A. Casein kinase I epsilon associates with and phosphorylates the tight junction protein occludin. FEBS Lett. 2006;580:2388-94 pubmed..We have identified casein kinase I epsilon (CKI epsilon) as a binding partner for the C-terminal cytoplasmic domain of occludin by yeast two-hybrid screening...
- Shirogane T, Jin J, Ang X, Harper J. SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein. J Biol Chem. 2005;280:26863-72 pubmed
- Hino S, Michiue T, Asashima M, Kikuchi A. Casein kinase I epsilon enhances the binding of Dvl-1 to Frat-1 and is essential for Wnt-3a-induced accumulation of beta-catenin. J Biol Chem. 2003;278:14066-73 pubmedWe demonstrate that Dvl-1, casein kinase I epsilon (CKI epsilon), and Frat-1 activate the Wnt signaling pathway cooperatively...
- Fish K, Cegielska A, Getman M, Landes G, Virshup D. Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family. J Biol Chem. 1995;270:14875-83 pubmed..Human CKI epsilon is a novel CKI isoform with properties that overlap those of previously described CKI isoforms.
- Keesler G, Camacho F, Guo Y, Virshup D, Mondadori C, Yao Z. Phosphorylation and destabilization of human period I clock protein by human casein kinase I epsilon. Neuroreport. 2000;11:951-5 pubmed..hPER I protein could also be co-immunoprecipitated with transfected hCKI epsilon as well as endogenous hCKI epsilon, indicating physical association between hPER I and hCKI epsilon proteins in vivo. ..
- Cajanek L, Ganji R, Henriques Oliveira C, Theofilopoulos S, Konik P, Bryja V, et al. Tiam1 regulates the Wnt/Dvl/Rac1 signaling pathway and the differentiation of midbrain dopaminergic neurons. Mol Cell Biol. 2013;33:59-70 pubmed publisher..In summary, our data identify Tiam1 as a novel regulator of DA neuron development and as a Dvl-associated and Rac1-specific GEF acting in the Wnt/Dvl/Rac1 pathway. ..
- Choksi D, Roy B, Chatterjee S, Yusuff T, Bakhoum M, Sengupta U, et al. TDP-43 Phosphorylation by casein kinase I? promotes oligomerization and enhances toxicity in vivo. Hum Mol Genet. 2014;23:1025-35 pubmed publisher..These data identify CKI? as a potent TDP-43 kinase in vivo and implicate oligomeric species as the toxic entities in TDP-43 proteinopathies...
- Dephoure N, Zhou C, Villen J, Beausoleil S, Bakalarski C, Elledge S, et al. A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008;105:10762-7 pubmed publisher..Analysis of non-proline site-containing phosphopeptides identified two unique motifs that suggest there are at least two undiscovered mitotic kinases. ..
- Xu Y, Toh K, Jones C, Shin J, Fu Y, Ptacek L. Modeling of a human circadian mutation yields insights into clock regulation by PER2. Cell. 2007;128:59-70 pubmed..Altering CKIdelta dosage modulates the S662 phenotype demonstrating that CKIdelta can regulate period through PER2 in vivo. Modeling a naturally occurring human variant in mice has yielded novel insights into PER2 regulation. ..
- Partch C, Shields K, Thompson C, Selby C, Sancar A. Posttranslational regulation of the mammalian circadian clock by cryptochrome and protein phosphatase 5. Proc Natl Acad Sci U S A. 2006;103:10467-10472 pubmed publisher..Collectively, these findings indicate that PP5, CKIepsilon, and cryptochrome dynamically regulate the mammalian circadian clock. ..
- Swiatek W, Kang H, Garcia B, Shabanowitz J, Coombs G, Hunt D, et al. Negative regulation of LRP6 function by casein kinase I epsilon phosphorylation. J Biol Chem. 2006;281:12233-41 pubmed..Generation of active CKIepsilon may induce a negative feedback loop by phosphorylation of sites on LRP5/6 that modulate axin binding and hence beta-catenin degradation. ..
- Okamura A, Iwata N, Nagata A, Tamekane A, Shimoyama M, Gomyo H, et al. Involvement of casein kinase Iepsilon in cytokine-induced granulocytic differentiation. Blood. 2004;103:2997-3004 pubmed
- Kishida M, Hino Si -, Michiue T, Yamamoto H, Kishida S, Fukui A, et al. Synergistic activation of the Wnt signaling pathway by Dvl and casein kinase Iepsilon. J Biol Chem. 2001;276:33147-55 pubmed..These results indicate that Dvl and CKIepsilon synergistically activated the Wnt signaling pathway and that the binding of the complex of Dvl and CKIepsilon to Axin is necessary for their synergistic action. ..
- Daub H, Olsen J, Bairlein M, Gnad F, Oppermann F, Körner R, et al. Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008;31:438-48 pubmed publisher..These results provide a vastly extended knowledge base for functional studies on kinases and their regulation through site-specific phosphorylation. ..
- Burkard T, Planyavsky M, Kaupe I, Breitwieser F, Burckstummer T, Bennett K, et al. Initial characterization of the human central proteome. BMC Syst Biol. 2011;5:17 pubmed publisher..All the data are made publicly available to help other researchers who, for instance, need to compare or link focused datasets to a common background. ..
- Li V, Ng S, Boersema P, Low T, Karthaus W, Gerlach J, et al. Wnt signaling through inhibition of ?-catenin degradation in an intact Axin1 complex. Cell. 2012;149:1245-56 pubmed publisher..Subsequently, newly synthesized ?-catenin can accumulate in a free cytosolic form and engage nuclear TCF transcription factors. ..
- Yin H, Laguna K, Li G, Kuret J. Dysbindin structural homologue CK1BP is an isoform-selective binding partner of human casein kinase-1. Biochemistry. 2006;45:5297-308 pubmed..These data suggest that the acidic domain of dysbindin and its paralogs in humans may function to recruit casein kinase-1 isoforms to protein complexes involved in multiple biological functions. ..