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A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin.

Publication ,  Journal Article
Kizhatil, K; Wu, Y-X; Sen, A; Bennett, V
Published in: J Neurosci
September 15, 2002

Doublecortin is a cytoplasmic protein mutated in the neuronal migration disorder X-linked lissencephaly. This study describes a novel activity of doublecortin in recognition of the FIGQY-phosphotyrosine motif present in the cytoplasmic domain of the L1 cell adhesion molecule neurofascin. Phospho-FIGQY-neurofascin (186 kDa) coimmunoprecipitated with doublecortin from detergent extracts of embryonic brain membranes, and this doublecortin-phospho-FIGQY neurofascin complex was disassociated by a synthetic phospho-FIGQY neurofascin peptide but not by a dephospho-FIGQY peptide. Doublecortin specifically recognized the phospho-FIGQY tyrosine in the context of a synthetic phospho-FIGQY neurofascin peptide and in phospho-FIGQY neurofascin isolated from cells treated with pervanadate. Mutations of doublecortin causing lissencephaly (R59H, D62N, and G253D) abolished binding to the phospho-FIGQY peptide and to phospho-FIGQY neurofascin. Finally, phospho-FIGQY neurofascin and doublecortin colocalize in developing axon tracts and in zones enriched in migrating neurons in the embryonic cerebral cortex. In the adult rostral migratory stream, doublecortin colocalizes in migrating neurons with a phospho-FIGQY bearing L1 CAM different from neurofascin. The finding that doublecortin associates with FIGQY-phosphorylated neurofascin provides the first connection of doublecortin with the plasma membrane and could be important for a function of doublecortin in directing neuronal migration.

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Published In

J Neurosci

DOI

EISSN

1529-2401

Publication Date

September 15, 2002

Volume

22

Issue

18

Start / End Page

7948 / 7958

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Transfection
  • Structure-Activity Relationship
  • Rats
  • Protein Structure, Tertiary
  • Protein Binding
  • Precipitin Tests
  • Phosphorylation
  • Peptide Fragments
  • Neuropeptides
 

Citation

APA
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ICMJE
MLA
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Kizhatil, K., Wu, Y.-X., Sen, A., & Bennett, V. (2002). A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin. J Neurosci, 22(18), 7948–7958. https://doi.org/10.1523/JNEUROSCI.22-18-07948.2002
Kizhatil, Krishnakumar, Yi-Xin Wu, Anindita Sen, and Vann Bennett. “A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin.J Neurosci 22, no. 18 (September 15, 2002): 7948–58. https://doi.org/10.1523/JNEUROSCI.22-18-07948.2002.
Kizhatil K, Wu Y-X, Sen A, Bennett V. A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin. J Neurosci. 2002 Sep 15;22(18):7948–58.
Kizhatil, Krishnakumar, et al. “A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin.J Neurosci, vol. 22, no. 18, Sept. 2002, pp. 7948–58. Pubmed, doi:10.1523/JNEUROSCI.22-18-07948.2002.
Kizhatil K, Wu Y-X, Sen A, Bennett V. A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin. J Neurosci. 2002 Sep 15;22(18):7948–7958.

Published In

J Neurosci

DOI

EISSN

1529-2401

Publication Date

September 15, 2002

Volume

22

Issue

18

Start / End Page

7948 / 7958

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Transfection
  • Structure-Activity Relationship
  • Rats
  • Protein Structure, Tertiary
  • Protein Binding
  • Precipitin Tests
  • Phosphorylation
  • Peptide Fragments
  • Neuropeptides