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par3 polarity

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https://www.readbyqxmd.com/read/27881661/par3-integrates-tiam1-and-phosphatidylinositol-3-kinase-signaling-to-change-apical-membrane-identity
#1
Travis R Ruch, David M Bryant, Keith E Mostov, Joanne N Engel
Pathogens can alter epithelial polarity by recruiting polarity proteins to the apical membrane, but how a change in protein localization is linked to polarity disruption is not clear. In this study we used chemically induced dimerization to rapidly relocalize proteins from the cytosol to the apical surface. We demonstrate that forced apical localization of Par3, which is normally restricted to tight junctions, is sufficient to alter apical membrane identity through its interactions with phosphatidylinositol 3-Kinase (PI3K) and the Rac1 guanine nucleotide exchange factor Tiam1...
November 23, 2016: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/27855669/expression-of-par3-polarity-protein-correlates-with-poor-prognosis-in-ovarian-cancer
#2
Hiroe Nakamura, Kazunori Nagasaka, Kei Kawana, Ayumi Taguchi, Yuriko Uehara, Mitsuyo Yoshida, Masakazu Sato, Haruka Nishida, Asaha Fujimoto, Tomoko Inoue, Katsuyuki Adachi, Takeshi Nagamatsu, Takahide Arimoto, Katsutoshi Oda, Yutaka Osuga, Tomoyuki Fujii
BACKGROUND: Previous studies have shown that the cell polarity protein partitioning defective 3 (Par3) plays an essential role in the formation of tight junctions and definition of apical-basal polarity. Aberrant function of this protein has been reported to be involved in epithelial-mesenchymal transition (EMT) and cancer invasion. The aim of this study was to examine the functional mechanism of Par3 in ovarian cancer. METHODS: First, we investigated the association between Par3 expression level and survival of 50 ovarian cancer patients...
November 17, 2016: BMC Cancer
https://www.readbyqxmd.com/read/27760826/pleckstrin-homology-ph-domain-leucine-rich-repeat-protein-phosphatase-controls-cell-polarity-by-negatively-regulating-the-activity-of-atypical-protein-kinase-c
#3
Xiaopeng Xiong, Xin Li, Yang-An Wen, Tianyan Gao
The proper establishment of epithelial polarity allows cells to sense and respond to signals that arise from the microenvironment in a spatiotemporally controlled manner. Atypical PKCs (aPKCs) are implicated as key regulators of epithelial polarity. However, the molecular mechanism underlying the negative regulation of aPKCs remains largely unknown. In this study, we demonstrated that PH domain leucine-rich repeat protein phosphatase (PHLPP), a novel family of Ser/Thr protein phosphatases, plays an important role in regulating epithelial polarity by controlling the phosphorylation of both aPKC isoforms...
November 25, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27624926/hook2-a-microtubule-binding-protein-interacts-with-par6%C3%AE-and-controls-centrosome-orientation-during-polarized-cell-migration
#4
Emilie Pallesi-Pocachard, Elsa Bazellieres, Annelise Viallat-Lieutaud, Marie-Hélène Delgrossi, Magali Barthelemy-Requin, André Le Bivic, Dominique Massey-Harroche
Polarity protein complexes function during polarized cell migration and a subset of these proteins localizes to the reoriented centrosome during this process. Despite these observations, the mechanisms behind the recruitment of these polarity complexes such as the aPKC/PAR6α complex to the centrosome are not well understood. Here we identify Hook2 as an interactor for the aPKC/PAR6α complex that functions to localize this complex at the centrosome. We first demonstrate that Hook2 is essential for the polarized Golgi re-orientation towards the migration front...
2016: Scientific Reports
https://www.readbyqxmd.com/read/27554858/apkc-inhibition-by-par3-cr3-flanking-regions-controls-substrate-access-and-underpins-apical-junctional-polarization
#5
Erika V Soriano, Marina E Ivanova, Georgina Fletcher, Philippe Riou, Philip P Knowles, Karin Barnouin, Andrew Purkiss, Brenda Kostelecky, Peter Saiu, Mark Linch, Ahmed Elbediwy, Svend Kjær, Nicola O'Reilly, Ambrosius P Snijders, Peter J Parker, Barry J Thompson, Neil Q McDonald
Atypical protein kinase C (aPKC) is a key apical-basal polarity determinant and Par complex component. It is recruited by Par3/Baz (Bazooka in Drosophila) into epithelial apical domains through high-affinity interaction. Paradoxically, aPKC also phosphorylates Par3/Baz, provoking its relocalization to adherens junctions (AJs). We show that Par3 conserved region 3 (CR3) forms a tight inhibitory complex with a primed aPKC kinase domain, blocking substrate access. A CR3 motif flanking its PKC consensus site disrupts the aPKC kinase N lobe, separating P-loop/αB/αC contacts...
August 22, 2016: Developmental Cell
https://www.readbyqxmd.com/read/27505675/loss-of-the-par3-polarity-protein-promotes-breast-tumorigenesis-and-metastasis
#6
Luke Martin McCaffrey, JoAnne Montalbano, Constantina Mihai, Ian G Macara
No abstract text is available yet for this article.
August 8, 2016: Cancer Cell
https://www.readbyqxmd.com/read/27466317/ve-cadherin-interacts-with-cell-polarity-protein-pals1-to-regulate-vascular-lumen-formation
#7
Benjamin F Brinkmann, Tim Steinbacher, Christian Hartmann, Daniel Kummer, Denise Pajonczyk, Fatemeh Mirzapourshafiyi, Masanori Nakayama, Thomas Weide, Volker Gerke, Klaus Ebnet
Blood vessel tubulogenesis requires the formation of stable cell-to-cell contacts and the establishment of apicobasal polarity of vascular endothelial cells. Cell polarity is regulated by highly conserved cell polarity protein complexes such as the Par3-aPKC-Par6 complex and the CRB3-Pals1-PATJ complex, which are expressed by many different cell types and regulate various aspects of cell polarity. Here we describe a functional interaction of VE-cadherin with the cell polarity protein Pals1. Pals1 directly interacts with VE-cadherin through a membrane-proximal motif in the cytoplasmic domain of VE-cadherin...
September 15, 2016: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/27463802/kshv-mediated-regulation-of-par3-and-snail-contributes-to-b-cell-proliferation
#8
Hem C Jha, Zhiguo Sun, Santosh K Upadhyay, Darine W El-Naccache, Rajnish K Singh, Sushil K Sahu, Erle S Robertson
Studies have suggested that Epithelial-Mesenchymal Transition (EMT) and transformation is an important step in progression to cancer. Par3 (partitioning-defective protein) is a crucial factor in regulating epithelial cell polarity. However, the mechanism by which the latency associated nuclear antigen (LANA) encoded by Kaposi's Sarcoma associated herpesvirus (KSHV) regulates Par3 and EMTs markers (Epithelial-Mesenchymal Transition) during viral-mediated B-cell oncogenesis has not been fully explored. Moreover, several studies have demonstrated a crucial role for EMT markers during B-cell malignancies...
July 2016: PLoS Pathogens
https://www.readbyqxmd.com/read/27462467/dual-function-of-partitioning-defective-3-in-the-regulation-of-yap-phosphorylation-and-activation
#9
Peng Zhang, Shuting Wang, Sai Wang, Jing Qiao, Lei Zhang, Zhe Zhang, Zhengjun Chen
Partitioning-defective 3 (Par3), a key component of the evolutionarily conserved polarity PAR complex (Par3/Par6/aPKC), controls cell polarity and contributes to cell migration, proliferation and tumor development. Emerging evidence indicates that cell polarity proteins function as upstream modulators that regulate the Hippo pathway. However, little is known about Par3's involvement in the Hippo pathway. Here, we find Par3 and YAP dynamically co-localize in different subcellular compartments; that is, the membrane, cytoplasm and nucleus, in a cell-density-dependent manner...
2016: Cell Discovery
https://www.readbyqxmd.com/read/27452221/essential-role-of-polarity-protein-par3-for-epidermal-homeostasis-through-regulation-of-barrier-function-keratinocyte-differentiation-and-stem-cell-maintenance
#10
Noelle J A Ali, Martim Dias Gomes, Ronja Bauer, Susanne Brodesser, Catherin Niemann, Sandra Iden
Partitioning-defective (Par) proteins contribute to multiprotein complexes that drive cell polarity and fate in invertebrates. Of these, the ternary Par3-atypical protein kinase C-Par6 polarity complex mediates asymmetry in various systems, whereas Par3 and aPKC/Par6 can also act independently. aPKC-λ has recently been implicated in epidermal differentiation and stem cell fate; however, whether Par3 contributes to the homeostasis of adult stratified epithelia is currently unknown. Here, we provide functional evidence that epidermal Par3 loss disturbed the inside-out skin barrier, coinciding with altered expression and localization of principle tight junction components, and that epidermal differentiation and thickness were increased...
July 21, 2016: Journal of Investigative Dermatology
https://www.readbyqxmd.com/read/27226486/conditional-knockout-of-polarity-complex-atypical-pkc%C3%AE-reveals-an-anti-inflammatory-function-mediated-by-nf-%C3%AE%C2%BAb
#11
Radia Forteza, Yolanda Figueroa, Anastasia Mashukova, Vipin Dulam, Pedro J Salas
The conserved proteins of the polarity complex made up of atypical PKC (aPKC, isoforms ι and ζ), Par6, and Par3 determine asymmetry in several cell types, from Caenorhabditis elegans oocytes to vertebrate epithelia and neurons. We previously showed that aPKC is down-regulated in intestinal epithelia under inflammatory stimulation. Further, expression of constitutively active PKCι decreases NF-κB activity in an epithelial cell line, the opposite of the effect reported in other cells. Here we tested the hypothesis that aPKC has a dual function in epithelia, inhibiting the NF-κB pathway in addition to having a role in apicobasal polarity...
July 15, 2016: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/27221061/a-new-functional-role-uncovered-for-rasgrf2-in-control-of-nuclear-migration-in-cone-photoreceptors-during-postnatal-retinal-development
#12
David Jimeno, Eugenio Santos
Despite their homologous structure and central nervous system(CNS) expression patterns, the GRF1 and GRF2 guanine nucleotide exchange factors(GEF) appear to play distinct, non-overlapping functions in cellular excitability, synaptic plasticity or neuromodulation. We recently uncovered a new functional role of GRF2 controlling nuclear migration in cone photoreceptors during postnatal neuroepithelial differentiation of the mouse retina. Analyzing GRF2-KO mice, we detected the specific accumulation of abnormally located, "ectopic" cone photoreceptor nuclei in the photoreceptor segment(PS) layer of their retinas...
May 24, 2016: Small GTPases
https://www.readbyqxmd.com/read/27151512/adherens-junction-and-e-cadherin-complex-regulation-by-epithelial-polarity
#13
REVIEW
Peter Coopman, Alexandre Djiane
E-Cadherin-based Adherens Junctions (AJs) are a defining feature of all epithelial sheets. Through the homophilic association of E-Cadherin molecules expressed on neighboring cells, they ensure intercellular adhesion amongst epithelial cells, and regulate many key aspects of epithelial biology. While their adhesive role requires these structures to remain stable, AJs are also extremely plastic. This plasticity allows for the adaptation of the cell to its changing environment: changes in neighbors after cell division, cell death, or cell movement, and changes in cell shape during differentiation...
September 2016: Cellular and Molecular Life Sciences: CMLS
https://www.readbyqxmd.com/read/27122542/par3a-is-dispensable-for-the-function-of-the-glomerular-filtration-barrier-of-the-kidney
#14
Sybille Koehler, Frederik Tellkamp, Carien M Niessen, Wilhelm Bloch, Dontscho Kerjaschki, Bernhard Schermer, Thomas Benzing, Paul T Brinkkoetter
Polarity signaling through the atypical PKC (aPKC)-Par polarity complex is essential for the development and maintenance of the podocyte architecture and the function of the glomerular filtration barrier of the kidney. To study the contribution of Par3A in this complex, we generated a novel Pard3 podocyte-specific knockout mouse model by targeting exon 6 of the Pard3 gene. Genetic deletion of Pard3a did not impair renal function, neither at birth nor later in life. Even challenging the animals did not result in glomerular disease...
July 1, 2016: American Journal of Physiology. Renal Physiology
https://www.readbyqxmd.com/read/27074039/magi-is-associated-with-the-par-complex-and-functions-antagonistically-with-bazooka-to-regulate-the-apical-polarity-complex
#15
Mojgan Padash Barmchi, Gayathri Samarasekera, Mary Gilbert, Vanessa J Auld, Bing Zhang
The mammalian MAGI proteins play important roles in the maintenance of adherens and tight junctions. The MAGI family of proteins contains modular domains such as WW and PDZ domains necessary for scaffolding of membrane receptors and intracellular signaling components. Loss of MAGI leads to reduced junction stability while overexpression of MAGI can lead to increased adhesion and stabilization of epithelial morphology. However, how Magi regulates junction assembly in epithelia is largely unknown. We investigated the single Drosophila homologue of Magi to study the in vivo role of Magi in epithelial development...
2016: PloS One
https://www.readbyqxmd.com/read/27072891/the-polarity-protein-par3-regulates-app-trafficking-and-processing-through-the-endocytic-adaptor-protein-numb
#16
Miao Sun, Suwaiba Z Asghar, Huaye Zhang
The processing of amyloid precursor protein (APP) into β-amyloid peptide (Aβ) is a key step in the pathogenesis of Alzheimer's disease (AD), and trafficking dysregulations of APP and its secretases contribute significantly to altered APP processing. Here we show that the cell polarity protein Par3 plays an important role in APP processing and trafficking. We found that the expression of full length Par3 is significantly decreased in AD patients. Overexpression of Par3 promotes non-amyloidogenic APP processing, while depletion of Par3 induces intracellular accumulation of Aβ...
September 2016: Neurobiology of Disease
https://www.readbyqxmd.com/read/27052178/pak4-is-required-during-epithelial-polarity-remodeling-through-regulating-aj-stability-and-bazooka-retention-at-the-za
#17
Rhian F Walther, Francisca Nunes de Almeida, Evi Vlassaks, Jemima J Burden, Franck Pichaud
The ability of epithelial cells to assemble into sheets relies on their zonula adherens (ZA), a circumferential belt of adherens junction (AJ) material, which can be remodeled during development to shape organs. Here, we show that during ZA remodeling in a model neuroepithelial cell, the Cdc42 effector P21-activated kinase 4 (Pak4/Mbt) regulates AJ morphogenesis and stability through β-catenin (β-cat/Arm) phosphorylation. We find that β-catenin phosphorylation by Mbt, and associated AJ morphogenesis, is needed for the retention of the apical determinant Par3/Bazooka at the remodeling ZA...
April 5, 2016: Cell Reports
https://www.readbyqxmd.com/read/26812085/cdc42-and-k-ras-control-endothelial-tubulogenesis-through-apical-membrane-and-cytoskeletal-polarization-novel-stimulatory-roles-for-gtpase-effectors-the-small-gtpases-rac2-and-rap1b-and-inhibitory-influence-of-arhgap31-and-rasa1
#18
Pieter R Norden, Dae Joong Kim, David M Barry, Ondine B Cleaver, George E Davis
A critical and understudied property of endothelial cells is their ability to form lumens and tube networks. Although considerable information has been obtained concerning these issues, including the role of Cdc42 and Rac1 and their effectors such as Pak2, Pak4, Par6b, and co-regulators such as integrins, MT1-MMP and Par3; many key questions remain that are necessary to elucidate molecular and signaling requirements for this fundamental process. In this work, we identify new small GTPase regulators of EC tubulogenesis including k-Ras, Rac2 and Rap1b that act in conjunction with Cdc42 as well as the key downstream effectors, IQGAP1, MRCKβ, beta-Pix, GIT1, and Rasip1 (which can assemble into multiprotein complexes with key regulators including α2β1 integrin and MT1-MMP)...
2016: PloS One
https://www.readbyqxmd.com/read/26685483/-atp6ap2-pro-renin-receptor-is-required-for-laminar-formation-during-retinal-development-in-mice
#19
REVIEW
Atsuhiro Kanda
(Pro) renin receptor [(P) RR], a key molecule for tissue renin-angiotensin system, was originally identified as Atp6ap2, an accessory subunit for vacuolar H(+)-ATPase that is a multi-subunit proton pump involved in fundamental cellular physiology. In this study, to elucidate the physiological functions of Atp6ap2/ (P) RR during retinal development in mammals, we used Cre-LoxP system to generate photoreceptor-specific conditional knock-out (CKO) mice, and revealed a critical role of Atp6ap2/(P) RR in photoreceptor development...
November 2015: Nippon Ganka Gakkai Zasshi
https://www.readbyqxmd.com/read/26589794/cancer-cell-invasion-in-three-dimensional-collagen-is-regulated-differentially-by-g%C3%AE-13-protein-and-discoidin-domain-receptor-1-par3-protein-signaling
#20
Christina R Chow, Kazumi Ebine, Lawrence M Knab, David J Bentrem, Krishan Kumar, Hidayatullah G Munshi
Cancer cells can invade in three-dimensional collagen as single cells or as a cohesive group of cells that require coordination of cell-cell junctions and the actin cytoskeleton. To examine the role of Gα13, a G12 family heterotrimeric G protein, in regulating cellular invasion in three-dimensional collagen, we established a novel method to track cell invasion by membrane type 1 matrix metalloproteinase-expressing cancer cells. We show that knockdown of Gα13 decreased membrane type 1 matrix metalloproteinase-driven proteolytic invasion in three-dimensional collagen and enhanced E-cadherin-mediated cell-cell adhesion...
January 22, 2016: Journal of Biological Chemistry
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