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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11 April 2005
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April 11 2005
Laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts
Shaohua Li,
Shaohua Li
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
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Patricia Liquari,
Patricia Liquari
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
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Karen K. McKee,
Karen K. McKee
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
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David Harrison,
David Harrison
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
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Raj Patel,
Raj Patel
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
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Sean Lee,
Sean Lee
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
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Peter D. Yurchenco
Peter D. Yurchenco
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
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Shaohua Li
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
Patricia Liquari
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
Karen K. McKee
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
David Harrison
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
Raj Patel
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
Sean Lee
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
Peter D. Yurchenco
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854
Correspondence to Peter D. Yurchenco: [email protected]
Abbreviations used in this paper: AEBSF, 4-(2-aminoethyl)benzenesulfonyl fluoride; BM, basement membrane; CS, circumsporozoite; DG, dystroglycan; ES, embryonic stem; gal-sulfatide, HSO3-3galactosylβ-1ceramide; glc-sulfatide, HSO3-3glucosylβ-1ceramide; Lm, laminin; MEF, mouse embryonic lung fibroblast; SC, Schwann cell.
Received:
January 19 2005
Accepted:
March 01 2005
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2005
J Cell Biol (2005) 169 (1): 179–189.
Article history
Received:
January 19 2005
Accepted:
March 01 2005
Citation
Shaohua Li, Patricia Liquari, Karen K. McKee, David Harrison, Raj Patel, Sean Lee, Peter D. Yurchenco; Laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts . J Cell Biol 11 April 2005; 169 (1): 179–189. doi: https://doi.org/10.1083/jcb.200501098
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