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- W2044799355 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." @default.
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- W2044799355 date "2003-05-20" @default.
- W2044799355 modified "2023-10-18" @default.
- W2044799355 title "Occludin phosphorylation: identification of an occludin kinase in brain and cell extracts as CK2" @default.
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- W2044799355 doi "https://doi.org/10.1016/s0014-5793(03)00525-8" @default.
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