The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation.

Published

Journal Article

Cell-cell recognition and patterning of cell contacts have a critical role in mediating reversible assembly of a variety of transcellular complexes in the nervous system. This study provides evidence for regulation of cell interactions through modulation of ankyrin binding to neurofascin, a member of the L1CAM family of nervous system cell adhesion molecules. The phosphorylation state of the conserved FIGQY tyrosine in the cytoplasmic domain of neurofascin regulates ankyrin binding and governs neurofascin-dependent cell aggregation as well as cell sorting when neurofascin is expressed in neuroblastoma cells. These findings suggest a general mechanism for the patterning of cell contact based on external signals that regulate tyrosine phosphorylation of L1CAM members and modulate their binding to ankyrin.

Full Text

Duke Authors

Cited Authors

  • Tuvia, S; Garver, TD; Bennett, V

Published Date

  • November 25, 1997

Published In

Volume / Issue

  • 94 / 24

Start / End Page

  • 12957 - 12962

PubMed ID

  • 9371782

Pubmed Central ID

  • 9371782

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.94.24.12957

Language

  • eng

Conference Location

  • United States