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. 2019 Dec 13;12:305. doi: 10.3389/fnmol.2019.00305

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Copyright © 2019 Yurchenco and McKee.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Neuromuscular Basement Membrane Assembly Steps. (A) Laminin becomes anchored to the cell surface by binding to integrins (α7β1 in muscle and several laminin-class integrins on Schwann cells) and α-dystroglycan (αDG) receptors. In Schwann cells, there are additional attachments mediated by sulfated glycolipids (SGLs). The three different LN domains of laminins bind to each other to form a planar polymer, creating an initial matrix scaffolding. Lm411 (a normal components of SC BMs) is unable to polymerize. (B) The G3 domains of nidogen-1 and -2 bind to the Lmγ1-LEb3 domain. Agrin binds to the coiled-coil domain of laminin and to αDG. Perlecan, another HSPG, binds to the nidogen G2 domain and to αDG. Collagen-IV binds to the G2 nidogen domain and forms a second polymer through covalent N- (7S) and C-(NC1) terminal domain bonds. Non-covalent lateral associations force the collagen into a tighter network.