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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Main Authors:	Li, Shaohua, Liquari, Patricia, McKee, Karen K., Harrison, David, Patel, Raj, Lee, Sean, Yurchenco, Peter D.
Format:	Online
Language:	English
Published:	The Rockefeller University Press 2005
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171891/

id	pubmed-2171891
recordtype	oai_dc
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. 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/).
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Li, Shaohua Liquari, Patricia McKee, Karen K. Harrison, David Patel, Raj Lee, Sean Yurchenco, Peter D.
spellingShingle	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
author_facet	Li, Shaohua Liquari, Patricia McKee, Karen K. Harrison, David Patel, Raj Lee, Sean Yurchenco, Peter D.
author_sort	Li, Shaohua
title	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_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_sort	laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in schwann cells and fibroblasts
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.
publisher	The Rockefeller University Press
publishDate	2005
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171891/
_version_	1611424744161148928

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

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