Results 251 to 260 of about 17,751,190 (266)

Nuclear Localization of the Tight Junction Protein ZO-2 in Epithelial Cells

Experimental Cell Research, 2002
The 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, Jesús, Vega, Lissette, Ponce, Lorenza, González-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, 2004
ZO-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, Arturo, Ponce, Jacqueline, Moreno, Abigail, Betanzos, Miriam, Huerta, Esther, Lopez-Bayghen, Lorenza, Gonzalez-Mariscal   +6 more
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Identification of a new protein that interacts with the tight junction protein ZO‐2

The FASEB Journal, 2008
The purpose of this study is to identify new proteins that interact with the middle portion of ZO‐2. We found a new protein pb3PSG (protein binding to 3PSG) and we want to characterize it in epithelial MDCK cells. We performed a two‐hybrid system using the 3PSG segment of ZO‐2 as bait.
Susana Lechuga, Jesus Solano, Lorenza Gonzalez‐Mariscal   +2 more
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Organization and expression of the human zo-2 gene (tjp-2) in normal and neoplastic tissues

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2000
One of the tight junction components, zonula occludens protein 2 (ZO-2), is expressed as two isoforms, ZO-2A and ZO-2C, in normal epithelia. In pancreatic adenocarcinoma of the ductal type ZO-2A is absent, but none of the common mechanisms of gene inactivation is responsible for lack of ZO-2A expression.
A, Chlenski, K V, Ketels, G I, Korovaitseva, M S, Talamonti, R, Oyasu, D G, Scarpelli   +5 more
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The tight junction protein ZO-2 has several functional nuclear export signals

Experimental Cell Research, 2006
The 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, Arturo, Ponce, Lourdes, Alarcón, Blanca Estela, Jaramillo   +3 more
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ZO‐2, a tight junction scaffold protein involved in the regulation of cell proliferation and apoptosis

Annals of the New York Academy of Sciences, 2012
ZO‐2 is a membrane‐associated guanylate kinase homologue (MAGUK) tight protein associated with the cytoplasmic surface of tight junctions. Here, we describe how ZO‐2 is a multidomain molecule that binds to a variety of cell signaling proteins, to the actin cytoskeleton, and to gap, tight, and adherens junction proteins.
Lorenza, Gonzalez-Mariscal, Pablo, Bautista, Susana, Lechuga, Miguel, Quiros   +3 more
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The organophosphate pesticide methamidophos opens the blood-testis barrier and covalently binds to ZO-2 in mice

Toxicology and Applied Pharmacology, 2018
Methamidophos (MET) is an organophosphate (OP) pesticide widely used in agriculture in developing countries. MET causes adverse effects in male reproductive function in humans and experimental animals, but the underlying mechanisms remain largely unknown.
José Mario Ortega-Olvera, Robert Winkler, Betzabet Quintanilla-Vega, Mineko Shibayama, Bibiana Chávez-Munguía, Dolores Martín-Tapia, Lourdes Alarcón, Lorenza González-Mariscal   +7 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, 2003
Occludin, 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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Papillomavirus E6 oncoprotein up-regulates occludin and ZO-2 expression in ovariectomized mice epidermis

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, Erika, Garay, Arturo, Raya-Sandino, Orlando, Vargas-Sierra, José, Díaz-Chávez, Marco, Popoca-Cuaya, Paul F, Lambert, Lorenza, González-Mariscal, Patricio, Gariglio   +8 more
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ZO‐2, a tight junction protein involved in gene expression, proliferation, apoptosis, and cell size regulation

Annals of the New York Academy of Sciences, 2017
ZO‐2 is a peripheral tight junction protein that belongs to the membrane‐associated guanylate kinase protein family. Here, we explain the modular and supramodular organization of ZO‐2 that allows it to interact with a wide variety of molecules, including cell–cell adhesion proteins, cytoskeletal components, and nuclear factors.
Lorenza, González-Mariscal, Jael, Miranda, Arturo, Raya-Sandino, Alaide, Domínguez-Calderón, Francisco, Cuellar-Perez   +4 more
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