Casein kinase Iε associates with and phosphorylates the tight junction protein occludin
Casein kinase Iε associates with and phosphorylates the tight junction protein occludin
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DOI：
10.1016/j.febslet.2006.03.048
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发表时间：
2006-04-17
期刊：
影响因子：
3.5
通讯作者：
Ridley, AJ
中科院分区：
文献类型：
--
作者：
McKenzie, JAG;Riento, K;Ridley, AJ
封闭蛋白是一种完整的膜蛋白，有助于紧密连接功能。通过酵母双杂交筛选，我们已经确定了酪蛋白激酶I β（CKI β）作为闭合蛋白C-末端胞质结构域的结合伴侣。CKI使occludin磷酸化，并与来自人内皮细胞的occludin共定位和共免疫沉淀。occludin的氨基酸265-318足以用于CKI β结合和磷酸化。occludin的C-末端48个氨基酸的缺失增加CKI β结合和磷酸化，表明该区域抑制CKI β结合。这些数据将CKI β鉴定为一种新的闭合蛋白激酶，其对于闭合蛋白的调节可能是重要的。(c)2006年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
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.