Binding of netrin-4 to laminin short arms regulates basement membrane assembly.

Fiona Schneiders, Barbara Maertens, Kerstin Böse, Yong Li, William J. Brunken, Mats Paulsson, Neil Smyth, Manuel Koch

Research output: Contribution to journalArticlepeer-review

69 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)23750-23758
Number of pages9
JournalJournal of Biological Chemistry
Issue number33
Publication statusPublished - 2007


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