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

Shaohua Li, Patricia Liquari, Karen K. McKee, David Harrison, Raj Patel, Sean Lee, Peter D. Yurchenco

Research output: Contribution to journalArticlepeer-review

108 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)179-189
Number of pages11
JournalJournal of Cell Biology
Volume169
Issue number1
DOIs
StatePublished - Apr 11 2005

All Science Journal Classification (ASJC) codes

  • Cell Biology

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