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Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell

Elisa Giannoni1, Francesca Buricchi, Giovanni Raugei

  • 1Dipartimento di Scienze Biochimiche, Viale Morgagni 50, 50134 Firenze, Italy.

Molecular and Cellular Biology
|July 19, 2005
PubMed

Insights

Src tyrosine kinases (Src) are activated by oxidation, not just phosphorylation. This redox regulation is crucial for cell adhesion and spreading, and also plays a key role in v-Src tumorigenic properties.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Cancer Research

Background:

  • Src tyrosine kinases are critical for cell adhesion and spreading.
  • Integrin ligation triggers intracellular messengers, including reactive oxygen species (ROS).
  • ROS mediate cytoskeleton rearrangement and cell spreading.

Purpose of the Study:

  • To investigate the role of Src oxidation in cell adhesion and spreading.
  • To determine the involvement of ROS in Src activation and tumorigenesis.
  • To explore redox regulation of Src activity.

Main Methods:

  • Investigated Src activation following integrin ligation.
  • Assessed the impact of antioxidant treatments and Src mutants on v-Src tumorigenic properties.
  • Analyzed Src oxidation and Tyr527 dephosphorylation dynamics.

Main Results:

  • Src tyrosine kinase is oxidized and activated after integrin ligation.
  • A late activation phase of Src correlates with ROS production and cell spreading.
  • Antioxidant treatments and oxidant-insensitive Src mutants reduce v-Src invasivity and growth.

Conclusions:

  • Redox regulation of Src activity, alongside phosphorylation, is essential for cell adhesion.
  • ROS are key mediators of v-Src-driven tumorigenic properties.
  • Targeting Src oxidation may offer therapeutic strategies for cancer.

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