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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Tight-junction protein zonula occludens 2 is a target of phosphorylation by protein kinase C.

Zonula occludens 2 (ZO-2) protein is a tight-junction phos phorylated protein that belongs to the membrane- associated guanylate kinase ('MAGUK') family. Here we study the interaction between ZO-2 and protein kinase C ( PKC). We have constructed two ZO-2 fusion proteins of the middle (3PSG) and C-terminal (AP) regions of the molecule and demonstrate that they are phosphorylated by PKC isoenzymes beta, epsilon, lambda and zeta. To understand the physiological significance of the interaction between ZO-2 and PKC, we analysed the phosphorylation state of ZO-2 immunoprecipitated from monolayers with mature tight junctions or from cells that either lack them or have them disassembled through Ca(2+) chelation. We found that in the latter condition the phosphorylation level of ZO-2 is significantly higher and is due to the action of both PKC and cAMP-dependent protein kinase. These results therefore suggest that the phosphorylated state of ZO-2 restrains its capacity to operate at the junctional complex.[1]

References

  1. Tight-junction protein zonula occludens 2 is a target of phosphorylation by protein kinase C. Avila-Flores, A., Rendón-Huerta, E., Moreno, J., Islas, S., Betanzos, A., Robles-Flores, M., González-Mariscal, L. Biochem. J. (2001) [Pubmed]
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