Casein kinase I epsilon associates with and phosphorylates the tight junction protein occludin.

Occludin is an integral-membrane protein that contributes to tight junction function. 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. CKI epsilon phosphorylated occludin and co-localised and co-immunoprecipitated with occludin from human endothelial cells. Amino ...
acids 265-318 of occludin were sufficient for CKI epsilon binding and phosphorylation. Deletion of the C-terminal 48 amino acids of occludin increased CKI epsilon binding and phosphorylation, suggesting that this region inhibits CKI epsilon binding. These data identify CKI epsilon as a novel occludin kinase that may be important for the regulation of occludin.
Mesh Terms:
Casein Kinase Iepsilon, Cells, Cultured, Endothelial Cells, Humans, Membrane Proteins, Occludin, Phosphorylation, Protein Binding, Protein Processing, Post-Translational, Protein Structure, Tertiary, Sequence Deletion, Tight Junctions, Two-Hybrid System Techniques
FEBS Lett.
Date: Apr. 17, 2006
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