The regulation of the expression, phosphorylation, and protein associations of pp125FAK during rat brain development

Mol Cell Neurosci. 1996 May;7(5):391-403. doi: 10.1006/mcne.1996.0028.

Abstract

We have studied both the expression and the interactions of focal adhesion kinase (FAK) during brain development. We have discovered that during different periods of development, FAK apparently has different properties. During the early stage of neurogenesis, FAK is phosphorylated, shows multiple isoforms, and interacts with the proto-oncogenes, src, fyn, and lyn. At this stage, FAK also interacts with both the N- and C-terminal SH2 domains of GAP, a negative regulator of the ras pathway. During later embryonic development, none of these protein interactions are apparent even though FAK is still predominantly phosphorylated. By adulthood FAK is largely unphosphorylated and migrates as a single protein species on SDS--PAGE. We discuss these results in terms of the dynamic cell movements that occur during embryonic brain development.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Age Factors
  • Animals
  • Astrocytes / cytology
  • Astrocytes / enzymology
  • Cell Adhesion Molecules / analysis
  • Cell Adhesion Molecules / biosynthesis*
  • Cell Adhesion Molecules / metabolism*
  • Cells, Cultured / enzymology
  • Cerebral Cortex / cytology*
  • Cerebral Cortex / embryology
  • Cerebral Cortex / growth & development
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Fetus / enzymology
  • Fetus / physiology
  • Fluorescent Antibody Technique
  • Focal Adhesion Kinase 1
  • Focal Adhesion Protein-Tyrosine Kinases
  • Glycosylation
  • Immunohistochemistry
  • Molecular Weight
  • Neurons / cytology
  • Neurons / enzymology
  • Phosphorylation
  • Pregnancy
  • Protein-Tyrosine Kinases / analysis
  • Protein-Tyrosine Kinases / biosynthesis*
  • Protein-Tyrosine Kinases / metabolism*
  • Rats
  • Rats, Sprague-Dawley
  • Receptor, Insulin / analysis
  • Receptor, Insulin / biosynthesis*
  • Receptor, Insulin / metabolism*
  • Signal Transduction / physiology
  • Tyrosine / metabolism

Substances

  • Cell Adhesion Molecules
  • Tyrosine
  • Protein-Tyrosine Kinases
  • Receptor, Insulin
  • Focal Adhesion Kinase 1
  • Focal Adhesion Protein-Tyrosine Kinases
  • Ptk2 protein, rat