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

Record type: Article

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.

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Citation

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 The Journal of Biological Chemistry, 282, (33), pp. 23750-23758. (doi:10.1074/jbc.M703137200).

More information

Published date: 1 August 2007

Identifiers

Local EPrints ID: 56054
URI: http://eprints.soton.ac.uk/id/eprint/56054
ISSN: 0021-9258
PURE UUID: b0ce38ba-2672-4784-b8d0-db24d578d65b

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Date deposited: 07 Aug 2008
Last modified: 17 Jul 2017 14:31

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Contributors

Author: F.I. Schneiders
Author: B. Maertens
Author: K. Bose
Author: Y. Li
Author: W.J. Brunken
Author: M. Paulsson
Author: N. Smyth
Author: M. Koch

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