Results 241 to 250 of about 67,145 (262)
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Experimental Cell Research, 2008
Apicolateral tight junctions (TJs) between epithelial cells are multiprotein complexes regulating membrane polarity and paracellular transport and also contribute to signalling pathways affecting cell proliferation and gene expression. ZO-2 and other ZO family members form a sub-membranous scaffold for binding TJ constituents.
Sheth, Bhavwanti +5 more
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Apicolateral tight junctions (TJs) between epithelial cells are multiprotein complexes regulating membrane polarity and paracellular transport and also contribute to signalling pathways affecting cell proliferation and gene expression. ZO-2 and other ZO family members form a sub-membranous scaffold for binding TJ constituents.
Sheth, Bhavwanti +5 more
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The tight junction protein ZO-2 has several functional nuclear export signals
Experimental Cell Research, 2006The tight junction (TJ) protein ZO-2 changes its subcellular distribution according to the state of confluency of the culture. Thus in confluent monolayers, it localizes at the TJ region whereas in sparse cultures it concentrates at the nucleus. The canine sequence of ZO-2 displays four putative nuclear export signals (NES), two at the second PDZ ...
Lorenza, González-Mariscal +3 more
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Nuclear Localization of the Tight Junction Protein ZO-2 in Epithelial Cells
Experimental Cell Research, 2002The tight junction constitutes the major barrier to solute and water flow through the paracellular space of epithelia and endothelia. It is formed by transmembrane proteins and submembranous molecules such as the MAGUKs ZOs. We have previously found that several MAGUKs, including those of the tight (ZO-1, ZO-2, and ZO-3) and septate junction (tamou and
Socorro, Islas +3 more
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Experimental Cell Research, 2013
We have studied the expression of the tight junction proteins (TJ) occludin, claudin-1 and ZO-2 in the epidermis of female mice. We observed a peak of expression of these proteins at postnatal day 7 and a decrease in 6 week-old mice to values similar to those found in newborn animals.
Jesús, Hernández-Monge +8 more
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We have studied the expression of the tight junction proteins (TJ) occludin, claudin-1 and ZO-2 in the epidermis of female mice. We observed a peak of expression of these proteins at postnatal day 7 and a decrease in 6 week-old mice to values similar to those found in newborn animals.
Jesús, Hernández-Monge +8 more
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Tyrosine phosphorylation of occludin attenuates its interactions with ZO-1, ZO-2, and ZO-3
Biochemical and Biophysical Research Communications, 2003Occludin, the transmembrane integral protein of the tight junction, plays a crucial role in the molecular organization and function of tight junction. While the homotypic interaction of extracellular loops of occludin appears to determine the barrier function of tight junction, the intracellular C-terminal tail, C-occludin, interacts with other tight ...
G, Kale, A P, Naren, P, Sheth, R K, Rao
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The Tight Junction Protein ZO‐2 Blocks Cell Cycle Progression and Inhibits Cyclin D1 Expression
Annals of the New York Academy of Sciences, 2009ZO‐2 is an adaptor protein of the tight junction that belongs to the MAGUK protein family. ZO‐2 is a dual localization protein that in sparse cultures is present at the cell borders and the nuclei, whereas in confluent cultures it is concentrated at the cell boundaries.
Lorenza, Gonzalez-Mariscal +3 more
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Characterization of the tight junction protein ZO-2 localized at the nucleus of epithelial cells
Experimental Cell Research, 2004ZO-2 is a MAGUK protein that in confluent epithelial sheets localizes at tight junctions (TJ) whereas in sparse cultures accumulates in clusters at the nucleus. Here, we have characterized several nuclear properties of ZO-2. We observe that ZO-2 is present in the nuclear matrix and co-immunoprecipitates with lamin B(1) and actin from the nuclei of ...
Blanca Estela, Jaramillo +6 more
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