PATJ regulates tight junction formation and polarity in mammalian epithelial cells

Shin, Kunyoo; Straight, Sam; Margolis, Ben

doi:10.1083/jcb.200408064

Cited by 183 publications

(216 citation statements)

References 32 publications

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“…However, Adachi et al (24) showed that, despite its domain similarity, mPATJ, but not MUPP1, regulates TJ stability (24). These data are in line with previous findings describing TJ formation delay or defects upon loss of mPATJ in cultured epithelial cells (25,26). Other studies describe a role of mPATJ in Myosin-driven processes like apical constriction and cell migration (27)(28)(29).…”

supporting

confidence: 80%

Localization and Function of Pals1-associated Tight Junction Protein in Drosophila Is Regulated by Two Distinct Apical Complexes

Sen

Sun

Krahn

2015

Journal of Biological Chemistry

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Background: Pals1-associated tight junction protein (PATJ) is an important regulator of Myosin-driven morphogenetic processes. Results: PATJ associates with two different apical complexes and accomplishes its function by a redundancy of its protein interaction domains. Conclusion:The correct targeting of PATJ to distinct apical domains is important for its function in Drosophila development. Significance: Learning how adaptor proteins can be regulated by protein targeting to distinct cellular compartments.

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supporting

confidence: 80%

Localization and Function of Pals1-associated Tight Junction Protein in Drosophila Is Regulated by Two Distinct Apical Complexes

Sen

Sun

Krahn

2015

Journal of Biological Chemistry

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“…However, the recovered PATJ is mislocalized in the L379P cell line and the delC cell line (Supplemental Figure 2). Our laboratory has done a PATJ knockdown and has not observed adherens junction disruption (Shin et al, 2005). A separate PATJ knockdown study in Caco2 cells reported that PATJ knockdown leads to the mislocalization of PALS1, but no adherens junction defect followed the PATJ depletion and PALS1 mislocalization (Michel et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

PALS1 Regulates E-Cadherin Trafficking in Mammalian Epithelial Cells

Wang¹,

Chen

Margolis

2007

MBoC

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Protein Associated with Lin Seven 1 (PALS1) is an evolutionarily conserved scaffold protein that targets to the tight junction in mammalian epithelia. Prior work in our laboratory demonstrated that the knockdown of PALS1 in Madin Darby canine kidney cells leads to tight junction and polarity defects. We have created new PALS1 stable knockdown cell lines with more profound reduction of PALS1 expression, and a more severe defect in tight junction formation was observed. Unexpectedly, we also observed a severe adherens junction defect, and both defects were corrected when PALS1 wild type and certain PALS1 mutants were expressed in the knockdown cells. We found that the adherens junction structural component E-cadherin was not effectively delivered to the cell surface in the PALS1 knockdown cells, and E-cadherin puncta accumulated in the cell periphery. The exocyst complex was also found to be mislocalized in PALS1 knockdown cells, potentially explaining why E-cadherin trafficking is disrupted. Our results suggest a broad and evolutionarily conserved role for the tight junction protein PALS1 in the biogenesis of adherens junction.

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“…These two effects on localization also yield distinct functional consequences. Evidence suggests that sequestered PDZ proteins are functionally inactivated because, in epithelial cells, E4-ORF1-induced sequestration of the PATJ polarity protein and ZO-2, which are critical for tight junction (TJ) biogenesis (Shin et al, 2005;Umeda et al, 2006), disrupts the TJ barrier function and causes a loss of apicobasal polarity (Latorre et al, 2005). In fibroblasts, sequestration of ZO-2 also blocks its tumor suppressor activity (Glaunsinger et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Functionally distinct monomers and trimers produced by a viral oncoprotein

et al. 2007

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While the process of homo-oligomer formation and disassembly into subunits represents a common strategy to regulate protein activity, reports of proteins in which the subunit and homo-oligomer perform independent functions are scarce. Tumorigenesis induced by the adenovirus E4-ORF1 oncoprotein depends on its binding to a select group of cellular PDZ proteins, including MUPP1, MAGI-1, ZO-2 and Dlg1. We report here that in cells E4-ORF1 exists as both a monomer and trimer and that monomers specifically bind and sequester MUPP1, MAGI-1 and ZO-2 within insoluble complexes whereas trimers specifically bind Dlg1 and promote its translocation to the plasma membrane. This work exposes a novel strategy wherein the oligomerization state of a protein not only determines the capacity to bind separate related targets but also couples the interactions to different functional consequences.

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PATJ regulates tight junction formation and polarity in mammalian epithelial cells

Cited by 183 publications

References 32 publications

Localization and Function of Pals1-associated Tight Junction Protein in Drosophila Is Regulated by Two Distinct Apical Complexes

Localization and Function of Pals1-associated Tight Junction Protein in Drosophila Is Regulated by Two Distinct Apical Complexes

PALS1 Regulates E-Cadherin Trafficking in Mammalian Epithelial Cells

Functionally distinct monomers and trimers produced by a viral oncoprotein

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