ArticleMolecular biology of the cell2009
Phosphorylation of zona occludens-2 by protein kinase C epsilon regulates its nuclear exportation.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- ZO-2 is a scaffold at the centriole and mitotic spindle poles that enhances microtubule stability and supports the proper development of mitotic spindles and cilia.Cell and tissue research · 2025Article
- Article
- Tight junction protein ZO-2 modulates the nuclear accumulation of transcription factor TEAD.Molecular biology of the cell · 2021Article
- ZO-2 Is a Master Regulator of Gene Expression, Cell Proliferation, Cytoarchitecture, and Cell Size.International journal of molecular sciences · 2019Review
- Activation of the CaMolecular biology of the cell · 2019Article
- SUMOylation regulates the intracellular fate of ZO-2.Cellular and molecular life sciences : CMLS · 2017Article
- Bryostatin-1 Restores Blood Brain Barrier Integrity following Blast-Induced Traumatic Brain Injury.Molecular neurobiology · 2015Article
- Article
- Vascular endothelial tight junctions and barrier function are disrupted by 15(S)-hydroxyeicosatetraenoic acid partly via protein kinase C ε-mediated zona occludens-1 phosphorylation at threonine 770/772.The Journal of biological chemistry · 2014Article
- Sorting nexin 27 (SNX27) associates with zonula occludens-2 (ZO-2) and modulates the epithelial tight junction.The Biochemical journal · 2013Article
- The intracellular fate of zonula occludens 2 is regulated by the phosphorylation of SR repeats and the phosphorylation/O-GlcNAcylation of S257.Molecular biology of the cell · 2013Article
- Beyond cell-cell adhesion: Emerging roles of the tight junction scaffold ZO-2.Tissue barriers · 2013Review
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Authors and funding
11 authors.
Funding
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Abstract
Here, we have analyzed the subcellular destiny of newly synthesized tight junction protein zona occludens (ZO)-2. After transfection in sparse cells, 74% of cells exhibit ZO-2 at the nucleus, and after 18 h the value decreases to 17%. The mutation S369A located within the nuclear exportation signal 1 of ZO-2 impairs the nuclear export of the protein. Because Ser369 represents a putative protein kinase C (PKC) phosphorylation site, we tested the effect of PKC inhibition and stimulation on the nuclear export of ZO-2. Our results strongly suggest that the departure of ZO-2 from the nucleus is regulated by phosphorylation at Ser369 by novel PKCepsilon. To test the route taken by ZO-2 from synthesis to the plasma membrane, we devised a novel nuclear microinjection assay in which the nucleus served as a reservoir for anti-ZO-2 antibody. Through this assay, we demonstrate that a significant amount of newly synthesized ZO-2 goes into the nucleus and is later relocated to the plasma membrane. These results constitute novel information for understanding the mechanisms that regulate the intracellular fate of ZO-2.
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