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FEBS Lett. 2003 Jun 19;545(2-3):161-6.

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

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


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 10000-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.

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