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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Oligopeptide Competition Assay for Phosphorylation Site Determination

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Focal adhesion kinase is negatively regulated by phosphorylation at tyrosine 407

Yangmi Lim1, Haein Park, Jihyun Jeon

  • 1Department of Life Sciences, Division of Molecular Life Sciences and Center for Cell Signaling Research, Ewha Womans University, Seoul 120-750.

The Journal of Biological Chemistry
|February 17, 2007
PubMed

Insights

Phosphorylation of Focal Adhesion Kinase (FAK) at Tyr(407) was found to decrease FAK activity. This novel finding suggests FAK Tyr(407) phosphorylation negatively regulates FAK

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Focal adhesion kinase (FAK) is a key regulator of signal transduction.
  • FAK activity is modulated by tyrosine phosphorylation at specific residues.
  • The functional role of FAK phosphorylation at Tyr(407) remained uncharacterized.

Purpose of the Study:

  • To investigate the function of FAK phosphorylation at Tyr(407).
  • To determine the impact of FAK Tyr(407) phosphorylation on FAK activity and cellular functions.

Main Methods:

  • Utilized NIH3T3 cells for transfection studies.
  • Employed phosphorylation-mimicking (FAK 407E) and non-phosphorylatable (FAK 407F) FAK mutants.
  • Assessed FAK autophosphorylation, in vitro kinase activity, and FAK-mediated cellular processes (adhesion, spreading, proliferation, migration).

Main Results:

  • FAK Tyr(407) phosphorylation increased under serum starvation, contact inhibition, and cell cycle arrest.
  • Phosphorylation-mimicking FAK 407E mutant decreased FAK Tyr(397) autophosphorylation and inhibited FAK activity and functions.
  • Non-phosphorylatable FAK 407F mutant showed opposite effects, indicating Tyr(407) phosphorylation's inhibitory role.

Conclusions:

  • FAK Tyr(407) phosphorylation negatively regulates FAK kinase activity.
  • This phosphorylation event inhibits FAK-mediated cellular functions including adhesion, spreading, proliferation, and migration.
  • FAK Tyr(407) phosphorylation represents a novel mechanism for FAK activity control.

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