ArticleThe Biochemical journal2001
Tight-junction protein zonula occludens 2 is a target of phosphorylation by protein kinase C.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Therapeutic hypothermia augments the restorative effects of PKC-β and Nox2 inhibition on an in vitro model of human blood-brain barrier.Metabolic brain disease · 2021Article
- Protective Effects of Baicalin on Peritoneal Tight Junctions in Piglets Challenged withMolecules (Basel, Switzerland) · 2021Article
- Activation of the CaMolecular biology of the cell · 2019Article
- Bicellular Tight Junctions and Wound Healing.International journal of molecular sciences · 2018Review
- PARP‑1 may be involved in hydroquinone‑induced apoptosis by poly ADP‑ribosylation of ZO‑2.Molecular medicine reports · 2017Article
- Biphasic modulation of paracellular claudin-5 expression in mouse brain endothelial cells is mediated through the phosphoinositide-3-kinase/AKT pathway.The Journal of pharmacology and experimental therapeutics · 2014Article
- Beyond cell-cell adhesion: Emerging roles of the tight junction scaffold ZO-2.Tissue barriers · 2013Review
- Article
- AMP-18 facilitates assembly and stabilization of tight junctions to protect the colonic mucosal barrier.Inflammatory bowel diseases · 2012Article
- Effects of Lactobacillus plantarum on gut barrier function in experimental obstructive jaundice.World journal of gastroenterology · 2012Article
- Protein kinase Cζ phosphorylates occludin and promotes assembly of epithelial tight junctions.The Biochemical journal · 2011Article
- Claudin-1 required for HCV virus entry has high potential for phosphorylation and O-glycosylation.Virology journal · 2011Article
- Protein kinase C activation modulates reversible increase in cortical blood-brain barrier permeability and tight junction protein expression during hypoxia and posthypoxic reoxygenation.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2010Article
- Phosphorylation of zona occludens-2 by protein kinase C epsilon regulates its nuclear exportation.Molecular biology of the cell · 2009Article
- Intramolecular interactions between the SRC homology 3 and guanylate kinase domains of discs large regulate its function in asymmetric cell division.The Journal of biological chemistry · 2009Article
- Protein kinase A-dependent step(s) in hepatitis C virus entry and infectivity.Journal of virology · 2008Article
- Epithelial junctions and polarity: complexes and kinases.Current opinion in nephrology and hypertension · 2008Review
- Phosphorylation of claudin-4 by PKCepsilon regulates tight junction barrier function in ovarian cancer cells.Experimental cell research · 2007Article
- Molecular characterization of lymphatic endothelial cells.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Altered expression of zonula occludens-2 precedes increased blood-brain barrier permeability in a murine model of fulminant hepatic failure.Journal of investigative surgery : the official journal of the Academy of Surgical ResearchArticle
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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