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Nectin-like proteins mediate axon–Schwann cell interactions along the internode and are essential for myelination
Axon–glial interactions are critical for the induction of myelination and the domain organization of myelinated fibers. Although molecular complexes that mediate these interactions in the nodal region are known, their counterparts along the internode are poorly defined. We report that neurons and Sc...
Autores principales: | , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064549/ https://www.ncbi.nlm.nih.gov/pubmed/17724124 http://dx.doi.org/10.1083/jcb.200705132 |
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author | Maurel, Patrice Einheber, Steven Galinska, Jolanta Thaker, Pratik Lam, Isabel Rubin, Marina B. Scherer, Steven S. Murakami, Yoshinuri Gutmann, David H. Salzer, James L. |
author_facet | Maurel, Patrice Einheber, Steven Galinska, Jolanta Thaker, Pratik Lam, Isabel Rubin, Marina B. Scherer, Steven S. Murakami, Yoshinuri Gutmann, David H. Salzer, James L. |
author_sort | Maurel, Patrice |
collection | PubMed |
description | Axon–glial interactions are critical for the induction of myelination and the domain organization of myelinated fibers. Although molecular complexes that mediate these interactions in the nodal region are known, their counterparts along the internode are poorly defined. We report that neurons and Schwann cells express distinct sets of nectin-like (Necl) proteins: axons highly express Necl-1 and -2, whereas Schwann cells express Necl-4 and lower amounts of Necl-2. These proteins are strikingly localized to the internode, where Necl-1 and -2 on the axon are directly apposed by Necl-4 on the Schwann cell; all three proteins are also enriched at Schmidt-Lanterman incisures. Binding experiments demonstrate that the Necl proteins preferentially mediate heterophilic rather than homophilic interactions. In particular, Necl-1 on axons binds specifically to Necl-4 on Schwann cells. Knockdown of Necl-4 by short hairpin RNA inhibits Schwann cell differentiation and subsequent myelination in cocultures. These results demonstrate a key role for Necl-4 in initiating peripheral nervous system myelination and implicate the Necl proteins as mediators of axo–glial interactions along the internode. |
format | Text |
id | pubmed-2064549 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-20645492008-02-27 Nectin-like proteins mediate axon–Schwann cell interactions along the internode and are essential for myelination Maurel, Patrice Einheber, Steven Galinska, Jolanta Thaker, Pratik Lam, Isabel Rubin, Marina B. Scherer, Steven S. Murakami, Yoshinuri Gutmann, David H. Salzer, James L. J Cell Biol Research Articles Axon–glial interactions are critical for the induction of myelination and the domain organization of myelinated fibers. Although molecular complexes that mediate these interactions in the nodal region are known, their counterparts along the internode are poorly defined. We report that neurons and Schwann cells express distinct sets of nectin-like (Necl) proteins: axons highly express Necl-1 and -2, whereas Schwann cells express Necl-4 and lower amounts of Necl-2. These proteins are strikingly localized to the internode, where Necl-1 and -2 on the axon are directly apposed by Necl-4 on the Schwann cell; all three proteins are also enriched at Schmidt-Lanterman incisures. Binding experiments demonstrate that the Necl proteins preferentially mediate heterophilic rather than homophilic interactions. In particular, Necl-1 on axons binds specifically to Necl-4 on Schwann cells. Knockdown of Necl-4 by short hairpin RNA inhibits Schwann cell differentiation and subsequent myelination in cocultures. These results demonstrate a key role for Necl-4 in initiating peripheral nervous system myelination and implicate the Necl proteins as mediators of axo–glial interactions along the internode. The Rockefeller University Press 2007-08-27 /pmc/articles/PMC2064549/ /pubmed/17724124 http://dx.doi.org/10.1083/jcb.200705132 Text en Copyright © 2007, 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 | Research Articles Maurel, Patrice Einheber, Steven Galinska, Jolanta Thaker, Pratik Lam, Isabel Rubin, Marina B. Scherer, Steven S. Murakami, Yoshinuri Gutmann, David H. Salzer, James L. Nectin-like proteins mediate axon–Schwann cell interactions along the internode and are essential for myelination |
title | Nectin-like proteins mediate axon–Schwann cell interactions along the internode and are essential for myelination |
title_full | Nectin-like proteins mediate axon–Schwann cell interactions along the internode and are essential for myelination |
title_fullStr | Nectin-like proteins mediate axon–Schwann cell interactions along the internode and are essential for myelination |
title_full_unstemmed | Nectin-like proteins mediate axon–Schwann cell interactions along the internode and are essential for myelination |
title_short | Nectin-like proteins mediate axon–Schwann cell interactions along the internode and are essential for myelination |
title_sort | nectin-like proteins mediate axon–schwann cell interactions along the internode and are essential for myelination |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064549/ https://www.ncbi.nlm.nih.gov/pubmed/17724124 http://dx.doi.org/10.1083/jcb.200705132 |
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