PALS1 Regulates E-Cadherin Trafficking in Mammalian Epithelial Cells

Wang, Qian; Chen, Xiao Wei; Margolis, Ben

doi:10.1091/mbc.e06-07-0651

Cited by 83 publications

(75 citation statements)

References 33 publications

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“…The truncated Drosophila Sdt protein localizes correctly within embryonic photoreceptor cells but fails to associate with the membrane in pupal and adult photoreceptor cells. In line with these findings, the C-terminus of mammalian Pals1 has been shown to be essential for tight junction formation and E-cadherin trafficking in a calcium-switch assay (Wang et al, 2007). Intramolecular conformational rearrangement caused by binding of GUK-4.1/Hook-SH3 has been predicted to be a common feature of MAGUK proteins (Nix et al, 2000;Tavares et al, 2001).…”

Section: Essential Role Of the Nok Guk Domain In Epithelial Polaritymentioning

confidence: 70%

“…Our observations reveal a previously unknown diversity of alternative multi-protein assembly compositions of the Crumbs-Nagie-oko and Par6-aPKC protein complexes that are highly dependent on the developmental context. domain with Par6 is not essential for the maintenance of epithelial polarity within mammalian Madin Darby canine kidney (MDCK) epithelial cells (Wang et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Divergent polarization mechanisms during vertebrate epithelial development mediated by the Crumbs complex protein Nagie oko

Bit‐Avragim

Hellwig

Rudolph

et al. 2008

Journal of Cell Science

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The zebrafish MAGUK protein Nagie oko is a member of the evolutionarily conserved Crumbs protein complex and functions as a scaffolding protein involved in the stabilization of multi-protein assemblies at the tight junction. During zebrafish embryogenesis, mutations in nagie oko cause defects in both epithelial polarity and cardiac morphogenesis. We used deletion constructs of Nagie oko in functional rescue experiments to define domains essential for cell polarity, maintenance of epithelial integrity and cardiac morphogenesis. Inability of Nagie oko to interact with Crumbs proteins upon deletion of the PDZ domain recreates all aspects of the nagie oko mutant phenotype. Consistent with this observation, apical localization of Nagie oko within the myocardium and neural tube is dependent on Oko meduzy/Crumbs2a. Disruption of direct interactions with Patj or Lin-7, two other members of the Crumbs protein complex, via the bipartite L27 domains produces only partial nagie oko mutant phenotypes and does not impair correct junctional localization of the truncated Nagie oko deletion protein within myocardial cells. Similarly, loss of the evolutionarily conserved region 1 domain, which mediates binding to Par6, causes only a subset of the nagie oko mutant epithelial phenotypes. Finally, deletion of the C-terminus, including the entire guanylate kinase and the SH3 domains, renders the truncated Nagie oko protein inactive and recreates all features of the nagie oko mutant phenotype when tested in functional complementation assays. Our observations reveal a previously unknown diversity of alternative multi-protein assembly compositions of the Crumbs–Nagie-oko and Par6-aPKC protein complexes that are highly dependent on the developmental context.

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Section: Essential Role Of the Nok Guk Domain In Epithelial Polaritymentioning

confidence: 70%

Section: Introductionmentioning

confidence: 99%

Divergent polarization mechanisms during vertebrate epithelial development mediated by the Crumbs complex protein Nagie oko

Bit‐Avragim

Hellwig

Rudolph

et al. 2008

Journal of Cell Science

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“…In MDCK cells, PALS1 is required for the formation of both tight and adherens junctions (Wang et al, 2007). These observations, together…”

Section: Mals-3 Is Localized Supra-apical To F-actin and Associates Wmentioning

confidence: 78%

MALS-3 regulates polarity and early neurogenesis in the developing cerebral cortex

et al. 2008

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Apicobasal polarity plays an important role in regulating asymmetric cell divisions by neural progenitor cells (NPCs) in invertebrates, but the role of polarity in mammalian NPCs is poorly understood. Here, we characterize the function of the PDZ domain protein MALS-3 in the developing cerebral cortex. We find that MALS-3 is localized to the apical domain of NPCs. Mice lacking all three MALS genes fail to localize the polarity proteins PATJ and PALS1 apically in NPCs, whereas the formation and maintenance of adherens junctions appears normal. In the absence of MALS proteins, early NPCs progressed more slowly through the cell cycle, and their daughter cells were more likely to exit the cell cycle and differentiate into neurons. Interestingly, these effects were transient; NPCs recovered normal cell cycle properties during late neurogenesis. Experiments in which MALS-3 was targeted to the entire membrane resulted in a breakdown of apicobasal polarity, loss of adherens junctions, and a slowing of the cell cycle. Our results suggest that MALS-3 plays a role in maintaining apicobasal polarity and is required for normal neurogenesis in the developing cortex.

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“…The p120-cadherin binding is strengthened by the interaction of p120 with nectin-associated afadin in a way depending on Rap1, a small GTPase known to be important for AJ formation (Kooistra et al 2007), and this results in the suppression of E-cadherin endocytosis (Hoshino et al 2005). A component of the tight junction, PALS1, can also regulate the cadherin trafficking: In PALS1-knocked-down epithelial cells, the exocyst complex is mislocalized, and E-cadherin puncta accumulate in the cell periphery (Wang et al 2007). Recently, the Cdc42-Par6-aPKC pathway was reported to stabilize the AJ via the control of Arp2/ 3-dependent endocytosis (Georgiou et al 2008;Leibfried et al 2008).…”

Section: Cadherin Expression and Recyclingmentioning

confidence: 99%