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).

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Original Publication URL: http://dx.doi.org/10.1074/jbc.M703137200

Description/Abstract

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.

Item Type: Article
ISSNs: 0021-9258 (print)
Related URLs:
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: University Structure - Pre August 2011 > School of Biological Sciences
ePrint ID: 56054
Date Deposited: 07 Aug 2008
Last Modified: 27 Mar 2014 18:38
URI: http://eprints.soton.ac.uk/id/eprint/56054

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