The β(2)-Subunit (AMOG) of Human Na(+), K(+)-ATPase Is a Homophilic Adhesion Molecule
The β(2) subunit of Na(+), K(+)-ATPase was originally identified as the adhesion molecule on glia (AMOG) that mediates the adhesion of astrocytes to neurons in the central nervous system and that is implicated in the regulation of neurite outgrowth and neuronal migration. While β(1) isoform have bee...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9322774/ https://www.ncbi.nlm.nih.gov/pubmed/35887102 http://dx.doi.org/10.3390/ijms23147753 |
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author | Roldán, María Luisa Ramírez-Salinas, Gema Lizbeth Martinez-Archundia, Marlet Cuellar-Perez, Francisco Vilchis-Nestor, Claudia Andrea Cancino-Diaz, Juan Carlos Shoshani, Liora |
author_facet | Roldán, María Luisa Ramírez-Salinas, Gema Lizbeth Martinez-Archundia, Marlet Cuellar-Perez, Francisco Vilchis-Nestor, Claudia Andrea Cancino-Diaz, Juan Carlos Shoshani, Liora |
author_sort | Roldán, María Luisa |
collection | PubMed |
description | The β(2) subunit of Na(+), K(+)-ATPase was originally identified as the adhesion molecule on glia (AMOG) that mediates the adhesion of astrocytes to neurons in the central nervous system and that is implicated in the regulation of neurite outgrowth and neuronal migration. While β(1) isoform have been shown to trans-interact in a species-specific mode with the β(1) subunit on the epithelial neighboring cell, the β(2) subunit has been shown to act as a recognition molecule on the glia. Nevertheless, none of the works have identified the binding partner of β(2) or described its adhesion mechanism. Until now, the interactions pronounced for β(2)/AMOG are heterophilic cis-interactions. In the present report we designed experiments that would clarify whether β(2) is a cell–cell homophilic adhesion molecule. For this purpose, we performed protein docking analysis, cell–cell aggregation, and protein–protein interaction assays. We observed that the glycosylated extracellular domain of β(2)/AMOG can make an energetically stable trans-interacting dimer. We show that CHO (Chinese Hamster Ovary) fibroblasts transfected with the human β(2) subunit become more adhesive and make large aggregates. The treatment with Tunicamycin in vivo reduced cell aggregation, suggesting the participation of N-glycans in that process. Protein–protein interaction assay in vivo with MDCK (Madin-Darby canine kidney) or CHO cells expressing a recombinant β(2) subunit show that the β(2) subunits on the cell surface of the transfected cell lines interact with each other. Overall, our results suggest that the human β(2) subunit can form trans-dimers between neighboring cells when expressed in non-astrocytic cells, such as fibroblasts (CHO) and epithelial cells (MDCK). |
format | Online Article Text |
id | pubmed-9322774 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-93227742022-07-27 The β(2)-Subunit (AMOG) of Human Na(+), K(+)-ATPase Is a Homophilic Adhesion Molecule Roldán, María Luisa Ramírez-Salinas, Gema Lizbeth Martinez-Archundia, Marlet Cuellar-Perez, Francisco Vilchis-Nestor, Claudia Andrea Cancino-Diaz, Juan Carlos Shoshani, Liora Int J Mol Sci Article The β(2) subunit of Na(+), K(+)-ATPase was originally identified as the adhesion molecule on glia (AMOG) that mediates the adhesion of astrocytes to neurons in the central nervous system and that is implicated in the regulation of neurite outgrowth and neuronal migration. While β(1) isoform have been shown to trans-interact in a species-specific mode with the β(1) subunit on the epithelial neighboring cell, the β(2) subunit has been shown to act as a recognition molecule on the glia. Nevertheless, none of the works have identified the binding partner of β(2) or described its adhesion mechanism. Until now, the interactions pronounced for β(2)/AMOG are heterophilic cis-interactions. In the present report we designed experiments that would clarify whether β(2) is a cell–cell homophilic adhesion molecule. For this purpose, we performed protein docking analysis, cell–cell aggregation, and protein–protein interaction assays. We observed that the glycosylated extracellular domain of β(2)/AMOG can make an energetically stable trans-interacting dimer. We show that CHO (Chinese Hamster Ovary) fibroblasts transfected with the human β(2) subunit become more adhesive and make large aggregates. The treatment with Tunicamycin in vivo reduced cell aggregation, suggesting the participation of N-glycans in that process. Protein–protein interaction assay in vivo with MDCK (Madin-Darby canine kidney) or CHO cells expressing a recombinant β(2) subunit show that the β(2) subunits on the cell surface of the transfected cell lines interact with each other. Overall, our results suggest that the human β(2) subunit can form trans-dimers between neighboring cells when expressed in non-astrocytic cells, such as fibroblasts (CHO) and epithelial cells (MDCK). MDPI 2022-07-14 /pmc/articles/PMC9322774/ /pubmed/35887102 http://dx.doi.org/10.3390/ijms23147753 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Roldán, María Luisa Ramírez-Salinas, Gema Lizbeth Martinez-Archundia, Marlet Cuellar-Perez, Francisco Vilchis-Nestor, Claudia Andrea Cancino-Diaz, Juan Carlos Shoshani, Liora The β(2)-Subunit (AMOG) of Human Na(+), K(+)-ATPase Is a Homophilic Adhesion Molecule |
title | The β(2)-Subunit (AMOG) of Human Na(+), K(+)-ATPase Is a Homophilic Adhesion Molecule |
title_full | The β(2)-Subunit (AMOG) of Human Na(+), K(+)-ATPase Is a Homophilic Adhesion Molecule |
title_fullStr | The β(2)-Subunit (AMOG) of Human Na(+), K(+)-ATPase Is a Homophilic Adhesion Molecule |
title_full_unstemmed | The β(2)-Subunit (AMOG) of Human Na(+), K(+)-ATPase Is a Homophilic Adhesion Molecule |
title_short | The β(2)-Subunit (AMOG) of Human Na(+), K(+)-ATPase Is a Homophilic Adhesion Molecule |
title_sort | β(2)-subunit (amog) of human na(+), k(+)-atpase is a homophilic adhesion molecule |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9322774/ https://www.ncbi.nlm.nih.gov/pubmed/35887102 http://dx.doi.org/10.3390/ijms23147753 |
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