PATJ regulates tight junction formation and polarity in mammalian epithelial cells
Recent studies have revealed an important role for tight junction protein complexes in epithelial cell polarity. One of these complexes contains the apical transmembrane protein, Crumbs, and two PSD95/discs large/zonula occludens domain proteins, protein associated with Lin seven 1 (PALS1)/Stardust...
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The Rockefeller University Press
2005
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pubmed-21718252008-03-05 PATJ regulates tight junction formation and polarity in mammalian epithelial cells Shin, Kunyoo Straight, Sam Margolis, Ben Research Articles Recent studies have revealed an important role for tight junction protein complexes in epithelial cell polarity. One of these complexes contains the apical transmembrane protein, Crumbs, and two PSD95/discs large/zonula occludens domain proteins, protein associated with Lin seven 1 (PALS1)/Stardust and PALS1-associated tight junction protein (PATJ). Although Crumbs and PALS1/Stardust are known to be important for cell polarization, recent studies have suggested that Drosophila PATJ is not essential and its function is unclear. Here, we find that PATJ is targeted to the apical region and tight junctions once cell polarization is initiated. We show using RNAi techniques that reduction in PATJ expression leads to delayed tight junction formation as well as defects in cell polarization. These effects are reversed by reintroduction of PATJ into these RNAi cells. This study provides new functional information on PATJ as a polarity protein and increases our understanding of the Crumbs–PALS1–PATJ complex function in epithelial polarity. The Rockefeller University Press 2005-02-28 /pmc/articles/PMC2171825/ /pubmed/15738264 http://dx.doi.org/10.1083/jcb.200408064 Text en Copyright © 2005, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
repository_type |
Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Shin, Kunyoo Straight, Sam Margolis, Ben |
spellingShingle |
Shin, Kunyoo Straight, Sam Margolis, Ben PATJ regulates tight junction formation and polarity in mammalian epithelial cells |
author_facet |
Shin, Kunyoo Straight, Sam Margolis, Ben |
author_sort |
Shin, Kunyoo |
title |
PATJ regulates tight junction formation and polarity in mammalian epithelial cells |
title_short |
PATJ regulates tight junction formation and polarity in mammalian epithelial cells |
title_full |
PATJ regulates tight junction formation and polarity in mammalian epithelial cells |
title_fullStr |
PATJ regulates tight junction formation and polarity in mammalian epithelial cells |
title_full_unstemmed |
PATJ regulates tight junction formation and polarity in mammalian epithelial cells |
title_sort |
patj regulates tight junction formation and polarity in mammalian epithelial cells |
description |
Recent studies have revealed an important role for tight junction protein complexes in epithelial cell polarity. One of these complexes contains the apical transmembrane protein, Crumbs, and two PSD95/discs large/zonula occludens domain proteins, protein associated with Lin seven 1 (PALS1)/Stardust and PALS1-associated tight junction protein (PATJ). Although Crumbs and PALS1/Stardust are known to be important for cell polarization, recent studies have suggested that Drosophila PATJ is not essential and its function is unclear. Here, we find that PATJ is targeted to the apical region and tight junctions once cell polarization is initiated. We show using RNAi techniques that reduction in PATJ expression leads to delayed tight junction formation as well as defects in cell polarization. These effects are reversed by reintroduction of PATJ into these RNAi cells. This study provides new functional information on PATJ as a polarity protein and increases our understanding of the Crumbs–PALS1–PATJ complex function in epithelial polarity. |
publisher |
The Rockefeller University Press |
publishDate |
2005 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171825/ |
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1611424723763200000 |