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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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Model of linker protein modification of laminin interactions in models of ambulatory and non-ambulatory laminin α2-deficiency (Yurchenco et al., 2018). (A) In the dy^2J/dy^2J mouse, Lm211 is unable to polymerize as a result of in-frame deletion within the α2LN domain leading to its degradation (Colognato and Yurchenco, 1999). αLNNd binds to the nidogen-binding locus (replacing nidogen), thus “restoring” polymerization. (B) In the Lama2 null mice, the compensatory Lm411 neither polymerizes nor binds to the key αDG receptor of muscle. Miniagrin binds to the coiled-coil (replacing native agrin) while αLNNd binds to the nidogen-binding locus. The combination of linker proteins enables polymerization and greatly enhances cytoskeletal anchorage such that the modified laminin behaves in a manner similar to Lm211.