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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...

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Autores principales: Gollan, Leora, Sabanay, Helena, Poliak, Sebastian, Berglund, Erik O., Ranscht, Barbara, Peles, Elior
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2002
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.
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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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