The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation.
Journal Article (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
- PMC24245
International Standard Serial Number (ISSN)
- 0027-8424
Digital Object Identifier (DOI)
- 10.1073/pnas.94.24.12957
Language
- eng
Conference Location
- United States