Binding of netrin-4 to laminin short arms regulates basement membrane assembly
Schneiders, F.I., Maertens, B., Bose, K., Li, Y., Brunken, W.J., Paulsson, M., Smyth, N. and Koch, M. (2007) Binding of netrin-4 to laminin short arms regulates basement membrane assembly. Journal of Biological Chemistry, 282, (33), 23750-23758. (doi:10.1074/jbc.M703137200).
Full text not available from this repository.
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 laminin1 and3 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.
|Digital Object Identifier (DOI):||doi:10.1074/jbc.M703137200|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Divisions:||University Structure - Pre August 2011 > School of Biological Sciences
|Date Deposited:||07 Aug 2008|
|Last Modified:||06 Aug 2015 02:45|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
Actions (login required)