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A functional FERM domain binding motif in neurofascin.

Authors: Gunn-Moore, FJ  Hill, M  Davey, F  Herron, LR  Tait, S  Sherman, D  Brophy, PJ 
Citation: Gunn-Moore FJ, etal., Mol Cell Neurosci. 2006 Dec;33(4):441-6. Epub 2006 Oct 12.
Pubmed: (View Article at PubMed) PMID:17045809
DOI: Full-text: DOI:10.1016/j.mcn.2006.09.003

The L1 family of transmembrane cell adhesion receptors are involved in the development of the nervous system and consist of L1, neuron-glial-related cell adhesion molecule and neurofascin. All three receptors have a short cytoplasmic tail which is known to bind to the cytoskeletal associated protein ankyrin. Ezrin is a cytoplasmic binding protein known to link plasma membrane proteins to the cytoskeleton and has been shown to be a binding partner for L1. Here we show that neurofascin can also interact directly with ezrin. However, the mechanism of interaction of L1 and neurofascin with ezrin is by different mechanisms. We also show that the neurofascin isoform, Nfasc155, co-localizes with ezrin in transfected HEK293 cells but also in interdigitating Schwann cells at the node of Ranvier.

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RGD Object Information
RGD ID: 7207801
Created: 2013-02-06
Species: All species
Last Modified: 2013-02-06
Status: ACTIVE



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