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

J A G McKenzie, K Riento, A J Ridley

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)

Abstract

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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved
Original languageEnglish
Pages (from-to)2388 - 2394
Number of pages7
JournalFEBS Letters
Volume580
Issue number9
DOIs
Publication statusPublished - 17 Apr 2006

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