Occludin phosphorylation: identification of an occludin kinase in brain and cell extracts as CK2 |
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Authors: | Smales Caroline Ellis Moira Baumber Rachel Hussain Nayer Desmond Howard Staddon James M |
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Affiliation: | Eisai London Research Laboratories Ltd., Bernard Katz Building, University College London, Gower Street, London, WC1E 6BT, UK. |
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Abstract: | 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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