Journal
JOURNAL OF CELL BIOLOGY
Volume 169, Issue 1, Pages 179-189Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200501098
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Funding
- NIDDK NIH HHS [R01 DK036425, DK36425, R37 DK036425] Funding Source: Medline
- NINDS NIH HHS [R01 NS038469, R01-NS38469] Funding Source: Medline
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Endoneurial laminins (Lms), beta 1-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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