| First Author | Schneiders FI | Year | 2007 |
| Journal | J Biol Chem | Volume | 282 |
| Issue | 33 | Pages | 23750-8 |
| PubMed ID | 17588941 | Mgi Jnum | J:124769 |
| Mgi Id | MGI:3722516 | Doi | 10.1074/jbc.M703137200 |
| Citation | Schneiders FI, et al. (2007) Binding of netrin-4 to laminin short arms regulates basement membrane assembly. J Biol Chem 282(33):23750-8 |
| abstractText | Netrins were first identified as neural guidance molecules, acting through receptors that are members of the DCC and UNC-5 family. All netrins share structural homology to the laminin N-terminal domains and the laminin epidermal growth factor-like domains of laminin short arms. Laminins use these domains to self-assemble into complex networks. Here we demonstrate that netrin-4 is a component of basement membranes and is integrated into the laminin polymer via interactions with the laminin gamma1 andgamma3 short arms. The binding is mediated through the laminin N-terminal domain of netrin-4. In contrast to netrin-4, other members of the netrin family do not bind to these laminin short arms. Moreover, a truncated form of netrin-4 completely inhibits laminin-111 self-assembly in vitro, and full-length netrin-4 can partially disrupt laminin self-interactions. When added to explant cultures, netrin-4 retards salivary gland branching morphogenesis. |
