High impact information on CSNK1E

• The amino acid region 228-250 of Dvl-1 was necessary for its binding to Frat-1, and the interaction of Dvl-1 with Frat-1 was enhanced by CKI epsilon [1].
• Furthermore, depletion of CKI epsilon reduced the Wnt-3a-induced accumulation of beta-catenin, although it did not affect the basal level of beta-catenin [1].
• These results indicate that CKI epsilon-dependent phosphorylation of Dvl enhances the formation of a complex of Dvl-1 with Frat-1 and that this complex leads to the activation of the Wnt signaling pathway [1].
• Depletion of CKI epsilon by double-stranded RNA interference in HeLa S3 cells led to the inhibition of Wnt-3a-induced phosphorylation of Dvl and the binding of Dvl-1 to Frat-1 [1].
• The mechanisms that regulate CKI epsilon activity and substrate specificity are not well understood [2].

Biological context of CSNK1E

• These mechanisms may serve to regulate CKI epsilon and related forms of CKI in the cell, perhaps in response to DNA damage [2].
• Casein kinase I epsilon (CKI epsilon) is a member of the CKI gene family, members of which are involved in the control of SV40 DNA replication, DNA repair, and cell metabolism [2].

Anatomical context of CSNK1E

• Northern blot analysis shows that hCKI epsilon is expressed in multiple human cell lines [3].
• CKI epsilon phosphorylated occludin and co-localised and co-immunoprecipitated with occludin from human endothelial cells [4].

Associations of CSNK1E with chemical compounds

• We used a double-blind, crossover design in healthy human volunteers to test association between polymorphisms in the CSNK1E region and subjective response to placebo, 10, or 20 mg of oral D-amphetamine [5].

Physical interactions of CSNK1E

• 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 [4].

Other interactions of CSNK1E

• We demonstrate that Dvl-1, casein kinase I epsilon (CKI epsilon), and Frat-1 activate the Wnt signaling pathway cooperatively [1].
• When co-transfected with wild-type hCKI epsilon, in 293T cells, hPER I showed a significant increase in phosphorylation as evidenced by a shift in molecular mass [6].
• Phosphatase treatment also activated CKI epsilon toward the novel substrates I kappa B alpha and Ets-1 [2].
• Amino acids 265-318 of occludin were sufficient for CKI epsilon binding and phosphorylation [4].

References