CRB2 completes a fully expressed Crumbs complex in the Retinal Pigment Epithelium
| Autor: | Juan Carlos Arévalo, Antonio E. Paniagua, Concepción Lillo, Ángela M. Jimeno, José Aijón, Saray López-Benito, Saúl Herranz-Martín, David Jimeno, Almudena Velasco |
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| Přispěvatelé: | Fundación Ramón Areces, Ministerio de Ciencia e Innovación (España), Junta de Castilla y León |
| Rok vydání: | 2015 |
| Předmět: |
Multidisciplinary
CRB1 Retinal pigment epithelium Membrane Glycoproteins Tight junction Cell Membrane Gene Expression Membrane Proteins Adherens Junctions Retinal Pigment Epithelium Biology eye diseases Article Cell biology Transport protein Cell membrane Adherens junction Mice Protein Transport medicine.anatomical_structure Membrane protein Cell polarity medicine Animals sense organs |
| Zdroj: | Scientific Reports Digital.CSIC. Repositorio Institucional del CSIC instname |
| ISSN: | 2045-2322 |
| Popis: | 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. This study was supported by grants from Fundación Ramón Areces and Ministerio de Ciencia e Innovación (BFU2008-04490/BFI). S.H.M received support from the Junta de Castilla y León PhD Program. |
| Databáze: | OpenAIRE |
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