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Biochem J. 2001 Dec 1;360(Pt 2):295-304.

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

Author information

1
Department of Physiology, Biophysics and Neuroscience, Center for Research and Advanced Studies (CINVESTAV), A. Postal 14-740, México D.F. 07000.

Abstract

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.

PMID:
11716757
PMCID:
PMC1222229
DOI:
10.1042/0264-6021:3600295
[Indexed for MEDLINE]
Free PMC Article

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