Occludin phosphorylation: identification of an occludin kinase in brain and cell extracts as CK2

FEBS Letters

Desmond, Howard¹  Staddon, James M¹  Baumber, Rachel¹  Ellis, Moira¹  Hussain, Nayer¹  Smales, Caroline¹ 

[1] Eisai London Research Laboratories Ltd., Bernard Katz Building, University College London, Gower Street, London WC1E 6BT, UK

关键词: Tight junction;    Inflammation;    Oedema;    Signal transduction;   

DOI  :  10.1016/S0014-5793(03)00525-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In epithelial and endothelial cells, tight junctions limit paracellular flux of ions, proteins and other macromolecules. However, mechanisms regulating tight junction function are not clear. Occludin, a tight junction protein, undergoes phosphorylation changes in several situations but little is known about occludin kinases. A recombinant C-terminal fragment of occludin is a substrate for a kinase in crude extracts of brain. This activity was purified about 10 000-fold and identified as CK2 (casein kinase 2) by peptide mass fingerprinting, immunoblotting and mutation of CK2 sites within the occludin sequence. CK2 is therefore a candidate kinase for regulation of occludin phosphorylation in vivo.

【 授权许可】

Unknown