A functional FERM domain binding motif in neurofascin

Francis James Gunn-Moore, Maria Hill, Fleur Dieneke Davey, Lissa Rocha Herron, S Tait, D Sherman, P J Brophy

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)

Abstract

The L1 family of transmembrane cell adhesion receptors are involved in the development of the nervous system and consist of L1, neuronglial-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. (c) 2006 Elsevier Inc. All rights reserved.

Original languageEnglish
Pages (from-to)441-446
Number of pages6
JournalMolecular and Cellular Neuroscience
Volume33
Issue number4
DOIs
Publication statusPublished - 15 Dec 2006

Keywords

  • neurofascin
  • 4.1 ezrin radixin moesin
  • CELL-ADHESION MOLECULE
  • ANKYRIN-BINDING
  • L1 FAMILY
  • RADIXIN
  • PROTEIN
  • EZRIN
  • MOESIN
  • ORGANIZATION
  • RANVIER
  • MEMBRANE

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