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CRB2 completes a fully expressed Crumbs complex in the Retinal Pigment Epithelium
The CRB proteins CRB1, CRB2 and CRB3 are members of the cell polarity complex Crumbs in mammals that together with Scribble and Par complexes stablish the polarity of a variety of cell types. Although many members of the Crumbs complex proteins are expressed in the retinal pigment epithelium (RPE),...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4585915/ https://www.ncbi.nlm.nih.gov/pubmed/26404741 http://dx.doi.org/10.1038/srep14504 |
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author | Paniagua, Antonio E. Herranz-Martín, Saúl Jimeno, David Jimeno, Ángela M. López-Benito, Saray Carlos Arévalo, Juan Velasco, Almudena Aijón, José Lillo, Concepción |
author_facet | Paniagua, Antonio E. Herranz-Martín, Saúl Jimeno, David Jimeno, Ángela M. López-Benito, Saray Carlos Arévalo, Juan Velasco, Almudena Aijón, José Lillo, Concepción |
author_sort | Paniagua, Antonio E. |
collection | PubMed |
description | The CRB proteins CRB1, CRB2 and CRB3 are members of the cell polarity complex Crumbs in mammals that together with Scribble and Par complexes stablish the polarity of a variety of cell types. Although many members of the Crumbs complex proteins are expressed in the retinal pigment epithelium (RPE), and even though the mRNA of CRB2 has been detected in ARPE-19 cells and in the RPE/Choroid, to date no CRB protein has yet been found in this tissue. To investigate this possibility, we generated an antibody that specifically recognize the mouse CRB2 protein, and we demonstrate the expression of CRB2 in mouse RPE. Confocal analysis shows that CRB2 is restricted to the apicolateral membrane of RPE cells, and more precisely, in the tight junctions. Our study identified CRB2 as the member of the CRB protein family that is present together with the rest of the components of the Crumbs complex in the RPE apico-lateral cell membrane. Considering that the functions of CRB proteins are decisive in the establishment and maintenance of cell-cell junctions in several epithelial-derived cell types, we believe that these findings are a relevant starting point for unraveling the functions that CRB2 might perform in the RPE. |
format | Online Article Text |
id | pubmed-4585915 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-45859152015-09-30 CRB2 completes a fully expressed Crumbs complex in the Retinal Pigment Epithelium Paniagua, Antonio E. Herranz-Martín, Saúl Jimeno, David Jimeno, Ángela M. López-Benito, Saray Carlos Arévalo, Juan Velasco, Almudena Aijón, José Lillo, Concepción Sci Rep Article The CRB proteins CRB1, CRB2 and CRB3 are members of the cell polarity complex Crumbs in mammals that together with Scribble and Par complexes stablish the polarity of a variety of cell types. Although many members of the Crumbs complex proteins are expressed in the retinal pigment epithelium (RPE), and even though the mRNA of CRB2 has been detected in ARPE-19 cells and in the RPE/Choroid, to date no CRB protein has yet been found in this tissue. To investigate this possibility, we generated an antibody that specifically recognize the mouse CRB2 protein, and we demonstrate the expression of CRB2 in mouse RPE. Confocal analysis shows that CRB2 is restricted to the apicolateral membrane of RPE cells, and more precisely, in the tight junctions. Our study identified CRB2 as the member of the CRB protein family that is present together with the rest of the components of the Crumbs complex in the RPE apico-lateral cell membrane. Considering that the functions of CRB proteins are decisive in the establishment and maintenance of cell-cell junctions in several epithelial-derived cell types, we believe that these findings are a relevant starting point for unraveling the functions that CRB2 might perform in the RPE. Nature Publishing Group 2015-09-25 /pmc/articles/PMC4585915/ /pubmed/26404741 http://dx.doi.org/10.1038/srep14504 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Paniagua, Antonio E. Herranz-Martín, Saúl Jimeno, David Jimeno, Ángela M. López-Benito, Saray Carlos Arévalo, Juan Velasco, Almudena Aijón, José Lillo, Concepción CRB2 completes a fully expressed Crumbs complex in the Retinal Pigment Epithelium |
title | CRB2 completes a fully expressed Crumbs complex in the Retinal Pigment Epithelium |
title_full | CRB2 completes a fully expressed Crumbs complex in the Retinal Pigment Epithelium |
title_fullStr | CRB2 completes a fully expressed Crumbs complex in the Retinal Pigment Epithelium |
title_full_unstemmed | CRB2 completes a fully expressed Crumbs complex in the Retinal Pigment Epithelium |
title_short | CRB2 completes a fully expressed Crumbs complex in the Retinal Pigment Epithelium |
title_sort | crb2 completes a fully expressed crumbs complex in the retinal pigment epithelium |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4585915/ https://www.ncbi.nlm.nih.gov/pubmed/26404741 http://dx.doi.org/10.1038/srep14504 |
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