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The Journal of Neuroscience, January 12, 2005, 25(2):395-403; doi:10.1523/JNEUROSCI.4097-04.2005

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Development/Plasticity/Repair
L1-Mediated Branching Is Regulated by Two Ezrin-Radixin-Moesin (ERM)-Binding Sites, the RSLE Region and a Novel Juxtamembrane ERM-Binding Region

Ling Cheng,^1,2 Kouichi Itoh,³ and Vance Lemmon^1,2

¹Department of Neurosciences, Case Western Reserve University, Cleveland, Ohio 44106, ²The Miami Project to Cure Paralysis, University of Miami, Miami, Florida 33136, and ³Laboratory of Molecular Pharmacology, Department of Pharmaceutical Technology, Faculty of Pharmaceutical Sciences at Kagawa Campus, Tokushima Bunri University, Sanuki-City, Kagawa 769-2193, Japan

We investigated how the neural cell adhesion molecule L1 mediates neurite outgrowth through L1-L1 homophilic interactions. Wild-type L1 and L1 with mutations in the cytoplasmic domain (CD) were introduced into L1 knock-out neurons, and transfected neurons were grown on an L1 substrate. Neurite length and branching were compared between wild-type L1 and L1CD mutations. Surprisingly, the L1CD is not required for L1-mediated neurite outgrowth but plays a critical role in neurite branching, through both the juxtamembrane region and the RSLE region. We demonstrate that both regions serve as ezrin-moesin-radixin-binding sites. A truncation mutant that deletes 110 of 114 amino acids of the L1CD still supports neurite outgrowth on an L1 substrate, suggesting that a coreceptor binds to L1 in cis and mediates neurite outgrowth and that L1-ankyrin interactions are not essential for neurite initiation or outgrowth. These data are consistent with a model in which L1 can influence L1-mediated neurite outgrowth and branching through both the L1CD and a coreceptor.

Key words: L1CAM; neurite outgrowth; ERM proteins; axon branching; juxtamembrane; ankyrin; adhesion

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Received Aug 1, 2004; revised November 18, 2004; accepted November 19, 2004.

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