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Laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts

Endoneurial laminins (Lms), β1-integrins, and dystroglycan (DG) are important for Schwann cell (SC) ensheathment and myelination of axons. We now show that SC expression of galactosyl-sulfatide, a Lm-binding glycolipid, precedes that of Lms in developing nerves. This glycolipid anchors Lm-1 and -2 t...

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Autores principales: Li, Shaohua, Liquari, Patricia, McKee, Karen K., Harrison, David, Patel, Raj, Lee, Sean, Yurchenco, Peter D.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171891/
https://www.ncbi.nlm.nih.gov/pubmed/15824137
http://dx.doi.org/10.1083/jcb.200501098
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author Li, Shaohua
Liquari, Patricia
McKee, Karen K.
Harrison, David
Patel, Raj
Lee, Sean
Yurchenco, Peter D.
author_facet Li, Shaohua
Liquari, Patricia
McKee, Karen K.
Harrison, David
Patel, Raj
Lee, Sean
Yurchenco, Peter D.
author_sort Li, Shaohua
collection PubMed
description Endoneurial laminins (Lms), β1-integrins, and dystroglycan (DG) are important for Schwann cell (SC) ensheathment and myelination of axons. We now show that SC expression of galactosyl-sulfatide, a Lm-binding glycolipid, precedes that of Lms in developing nerves. This glycolipid anchors Lm-1 and -2 to SC surfaces by binding to their LG domains and enables basement membrane (BM) assembly. Revealingly, non–BM-forming fibroblasts become competent for BM assembly when sulfatides are intercalated into their cell surfaces. Assembly is characterized by coalescence of sulfatide, DG, and c-Src into a Lm-associated complex; by DG-dependent recruitment of utrophin and Src activation; and by integrin-dependent focal adhesion kinase phosphorylation. Collectively, our findings suggest that sulfated glycolipids are key Lm anchors that determine which cell surfaces can assemble Lms to initiate BM assembly and DG- and integrin-mediated signaling.
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spelling pubmed-21718912008-03-05 Laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts Li, Shaohua Liquari, Patricia McKee, Karen K. Harrison, David Patel, Raj Lee, Sean Yurchenco, Peter D. J Cell Biol Research Articles Endoneurial laminins (Lms), β1-integrins, and dystroglycan (DG) are important for Schwann cell (SC) ensheathment and myelination of axons. We now show that SC expression of galactosyl-sulfatide, a Lm-binding glycolipid, precedes that of Lms in developing nerves. This glycolipid anchors Lm-1 and -2 to SC surfaces by binding to their LG domains and enables basement membrane (BM) assembly. Revealingly, non–BM-forming fibroblasts become competent for BM assembly when sulfatides are intercalated into their cell surfaces. Assembly is characterized by coalescence of sulfatide, DG, and c-Src into a Lm-associated complex; by DG-dependent recruitment of utrophin and Src activation; and by integrin-dependent focal adhesion kinase phosphorylation. Collectively, our findings suggest that sulfated glycolipids are key Lm anchors that determine which cell surfaces can assemble Lms to initiate BM assembly and DG- and integrin-mediated signaling. The Rockefeller University Press 2005-04-11 /pmc/articles/PMC2171891/ /pubmed/15824137 http://dx.doi.org/10.1083/jcb.200501098 Text en Copyright © 2005, 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
Li, Shaohua
Liquari, Patricia
McKee, Karen K.
Harrison, David
Patel, Raj
Lee, Sean
Yurchenco, Peter D.
Laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts
title Laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts
title_full Laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts
title_fullStr Laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts
title_full_unstemmed Laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts
title_short Laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts
title_sort laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in schwann cells and fibroblasts
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171891/
https://www.ncbi.nlm.nih.gov/pubmed/15824137
http://dx.doi.org/10.1083/jcb.200501098
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