Skip to main content
Journal cover image

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

Publication ,  Journal Article
Tuvia, S; Garver, TD; Bennett, V
Published in: Proc Natl Acad Sci U S A
November 25, 1997

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.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

November 25, 1997

Volume

94

Issue

24

Start / End Page

12957 / 12962

Location

United States

Related Subject Headings

  • Tyrosine
  • Tumor Cells, Cultured
  • Protein Binding
  • Phosphorylation
  • Nerve Growth Factors
  • Molecular Sequence Data
  • Cytoplasm
  • Cell Separation
  • Cell Aggregation
  • Cell Adhesion Molecules
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Tuvia, S., Garver, T. D., & Bennett, V. (1997). The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation. Proc Natl Acad Sci U S A, 94(24), 12957–12962. https://doi.org/10.1073/pnas.94.24.12957
Tuvia, S., T. D. Garver, and V. Bennett. “The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation.Proc Natl Acad Sci U S A 94, no. 24 (November 25, 1997): 12957–62. https://doi.org/10.1073/pnas.94.24.12957.
Tuvia S, Garver TD, Bennett V. The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation. Proc Natl Acad Sci U S A. 1997 Nov 25;94(24):12957–62.
Tuvia, S., et al. “The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation.Proc Natl Acad Sci U S A, vol. 94, no. 24, Nov. 1997, pp. 12957–62. Pubmed, doi:10.1073/pnas.94.24.12957.
Tuvia S, Garver TD, Bennett V. The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation. Proc Natl Acad Sci U S A. 1997 Nov 25;94(24):12957–12962.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

November 25, 1997

Volume

94

Issue

24

Start / End Page

12957 / 12962

Location

United States

Related Subject Headings

  • Tyrosine
  • Tumor Cells, Cultured
  • Protein Binding
  • Phosphorylation
  • Nerve Growth Factors
  • Molecular Sequence Data
  • Cytoplasm
  • Cell Separation
  • Cell Aggregation
  • Cell Adhesion Molecules