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Nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core PCP factors to E-cadherin–β-catenin
Frizzled/planar cell polarity (PCP) signaling regulates cell motility in several tissues, including ommatidial rotation in Drosophila melanogaster. The Nemo kinase has also been linked to cell motility regulation and ommatidial rotation. The mechanistic role(s) of Nemo during rotation remain however...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3109122/ https://www.ncbi.nlm.nih.gov/pubmed/21552260 http://dx.doi.org/10.1038/nsmb.2049 |
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author | Mirkovic, Ivana Gault, William J. Rahnama, Maryam Jenny, Andreas Gaengel, Konstantin Bessette, Darrell Gottardi, Cara J. Verheyen, Esther M. Mlodzik, Marek |
author_facet | Mirkovic, Ivana Gault, William J. Rahnama, Maryam Jenny, Andreas Gaengel, Konstantin Bessette, Darrell Gottardi, Cara J. Verheyen, Esther M. Mlodzik, Marek |
author_sort | Mirkovic, Ivana |
collection | PubMed |
description | Frizzled/planar cell polarity (PCP) signaling regulates cell motility in several tissues, including ommatidial rotation in Drosophila melanogaster. The Nemo kinase has also been linked to cell motility regulation and ommatidial rotation. The mechanistic role(s) of Nemo during rotation remain however obscure. We demonstrate that nemo functions throughout the entire rotation movement promoting rate of rotation. Genetic and molecular studies indicate that Nemo binds both the core PCP factor complex of Strabismus–Prickle, and the E-cadherin–β-catenin (Armadillo) complex, which colocalize and like Nemo also promote rotation. Strabismus/Vang binds and stabilizes Nemo asymmetrically within the ommatidial precluster. Nemo and β-catenin then act synergistically promoting rotation, which is mediated in vivo through Nemo phosphorylation of β-catenin. Our data suggest that Nemo serves as a conserved molecular link between core PCP factors and E-cad/β-catenin complexes, promoting ommatidial rotation and cell motility in general. |
format | Online Article Text |
id | pubmed-3109122 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
record_format | MEDLINE/PubMed |
spelling | pubmed-31091222011-12-01 Nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core PCP factors to E-cadherin–β-catenin Mirkovic, Ivana Gault, William J. Rahnama, Maryam Jenny, Andreas Gaengel, Konstantin Bessette, Darrell Gottardi, Cara J. Verheyen, Esther M. Mlodzik, Marek Nat Struct Mol Biol Article Frizzled/planar cell polarity (PCP) signaling regulates cell motility in several tissues, including ommatidial rotation in Drosophila melanogaster. The Nemo kinase has also been linked to cell motility regulation and ommatidial rotation. The mechanistic role(s) of Nemo during rotation remain however obscure. We demonstrate that nemo functions throughout the entire rotation movement promoting rate of rotation. Genetic and molecular studies indicate that Nemo binds both the core PCP factor complex of Strabismus–Prickle, and the E-cadherin–β-catenin (Armadillo) complex, which colocalize and like Nemo also promote rotation. Strabismus/Vang binds and stabilizes Nemo asymmetrically within the ommatidial precluster. Nemo and β-catenin then act synergistically promoting rotation, which is mediated in vivo through Nemo phosphorylation of β-catenin. Our data suggest that Nemo serves as a conserved molecular link between core PCP factors and E-cad/β-catenin complexes, promoting ommatidial rotation and cell motility in general. 2011-05-08 2011-06 /pmc/articles/PMC3109122/ /pubmed/21552260 http://dx.doi.org/10.1038/nsmb.2049 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Mirkovic, Ivana Gault, William J. Rahnama, Maryam Jenny, Andreas Gaengel, Konstantin Bessette, Darrell Gottardi, Cara J. Verheyen, Esther M. Mlodzik, Marek Nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core PCP factors to E-cadherin–β-catenin |
title | Nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core PCP factors to E-cadherin–β-catenin |
title_full | Nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core PCP factors to E-cadherin–β-catenin |
title_fullStr | Nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core PCP factors to E-cadherin–β-catenin |
title_full_unstemmed | Nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core PCP factors to E-cadherin–β-catenin |
title_short | Nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core PCP factors to E-cadherin–β-catenin |
title_sort | nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core pcp factors to e-cadherin–β-catenin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3109122/ https://www.ncbi.nlm.nih.gov/pubmed/21552260 http://dx.doi.org/10.1038/nsmb.2049 |
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