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Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr
An axonal complex of cell adhesion molecules consisting of Caspr and contactin has been found to be essential for the generation of the paranodal axo-glial junctions flanking the nodes of Ranvier. Here we report that although the extracellular region of Caspr was sufficient for directing it to the p...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2002
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173544/ https://www.ncbi.nlm.nih.gov/pubmed/12082082 http://dx.doi.org/10.1083/jcb.200203050 |
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author | Gollan, Leora Sabanay, Helena Poliak, Sebastian Berglund, Erik O. Ranscht, Barbara Peles, Elior |
author_facet | Gollan, Leora Sabanay, Helena Poliak, Sebastian Berglund, Erik O. Ranscht, Barbara Peles, Elior |
author_sort | Gollan, Leora |
collection | PubMed |
description | An axonal complex of cell adhesion molecules consisting of Caspr and contactin has been found to be essential for the generation of the paranodal axo-glial junctions flanking the nodes of Ranvier. Here we report that although the extracellular region of Caspr was sufficient for directing it to the paranodes in transgenic mice, retention of the Caspr–contactin complex at the junction depended on the presence of an intact cytoplasmic domain of Caspr. Using immunoelectron microscopy, we found that a Caspr mutant lacking its intracellular domain was often found within the axon instead of the junctional axolemma. We further show that a short sequence in the cytoplasmic domain of Caspr mediated its binding to the cytoskeleton-associated protein 4.1B. Clustering of contactin on the cell surface induced coclustering of Caspr and immobilized protein 4.1B at the plasma membrane. Furthermore, deletion of the protein 4.1B binding site accelerated the internalization of a Caspr–contactin chimera from the cell surface. These results suggest that Caspr serves as a “transmembrane scaffold” that stabilizes the Caspr/contactin adhesion complex at the paranodal junction by connecting it to cytoskeletal components within the axon. |
format | Text |
id | pubmed-2173544 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21735442008-05-01 Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr Gollan, Leora Sabanay, Helena Poliak, Sebastian Berglund, Erik O. Ranscht, Barbara Peles, Elior J Cell Biol Article An axonal complex of cell adhesion molecules consisting of Caspr and contactin has been found to be essential for the generation of the paranodal axo-glial junctions flanking the nodes of Ranvier. Here we report that although the extracellular region of Caspr was sufficient for directing it to the paranodes in transgenic mice, retention of the Caspr–contactin complex at the junction depended on the presence of an intact cytoplasmic domain of Caspr. Using immunoelectron microscopy, we found that a Caspr mutant lacking its intracellular domain was often found within the axon instead of the junctional axolemma. We further show that a short sequence in the cytoplasmic domain of Caspr mediated its binding to the cytoskeleton-associated protein 4.1B. Clustering of contactin on the cell surface induced coclustering of Caspr and immobilized protein 4.1B at the plasma membrane. Furthermore, deletion of the protein 4.1B binding site accelerated the internalization of a Caspr–contactin chimera from the cell surface. These results suggest that Caspr serves as a “transmembrane scaffold” that stabilizes the Caspr/contactin adhesion complex at the paranodal junction by connecting it to cytoskeletal components within the axon. The Rockefeller University Press 2002-06-24 /pmc/articles/PMC2173544/ /pubmed/12082082 http://dx.doi.org/10.1083/jcb.200203050 Text en Copyright © 2002, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Gollan, Leora Sabanay, Helena Poliak, Sebastian Berglund, Erik O. Ranscht, Barbara Peles, Elior Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr |
title | Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr |
title_full | Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr |
title_fullStr | Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr |
title_full_unstemmed | Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr |
title_short | Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr |
title_sort | retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of caspr |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173544/ https://www.ncbi.nlm.nih.gov/pubmed/12082082 http://dx.doi.org/10.1083/jcb.200203050 |
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