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First published online 17 July 2006
doi: 10.1242/jcs.03057

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1ß1-integrin engagement to distinct laminin-1 domains orchestrates spreading, migration and survival of neural crest cells through independent signaling pathways

Nathalie Desban^1,*, Jean-Claude Lissitzky², Patricia Rousselle³ and Jean-Loup Duband^1,

¹ Laboratoire de Biologie du Développement, CNRS et Université Pierre et Marie Curie, 9 quai Saint-Bernard, 75252 Paris Cedex 05, France
² Unité Mixte de Recherche 6032, CNRS et Université de la Méditerranée, Facultés de Médecine et de Pharmacie, Marseille, France
³ IFR 128 BiosSciences Lyon-Gerland, Institut de Biologie et Chimie des Protéines, CNRS et Université Lyon-1, Lyon, France

Author for correspondence (e-mail: duband{at}ccr.jussieu.fr)

Accepted 18 May 2006

Integrin engagement regulates cell adhesion, shape, migration, growth, and differentiation, but molecular mechanisms coordinating these functions in cells remain unclear. Because of their migratory and differentiation potential, neural crest cells constitute a powerful paradigm to address this question. Here, we describe that laminin-1, a major component of their migration routes, promotes crest cell spreading, migration and survival through two distinct integrin-binding domains that are situated on both sides of its 1 subunit and can be separated in the LN-1 elastase proteolytic fragments E1' and E8. Interaction with either domain was mediated by the same integrin 1ß1 but produced distinct, complementary responses through specific signaling cascades. FAK activation upon E8 binding induced spreading, formation of actin bundles and focal adhesions, stimulated oriented migration, but failed to support survival. Conversely, Erk activation upon E1' binding promoted long-term survival and random migration without actin reorganization. Consistent with this, interaction with laminin-5 or laminin-10/11, which do not harbor integrin-binding domains in the N-terminal side of their chains, failed to support survival. Thus, the signaling activity and function of integrins might depend on binding domains in their ligands, thereby revealing ligand control of integrin function as a possible mechanism for the modulation and coordination of cell response to adhesive signals.

Key words: Neural crest, Integrin, Laminin, Cell migration, Cell survival, Signaling pathways

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