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The interaction of the tyrosine kinase pp60src with membrane and cytoskeletal components

S Kellie1, A R Horvath, G Felice

  • 1Yamanouchi Research Institute, Littlemore Hospital, Oxford, UK.

Symposia of the Society for Experimental Biology
|January 1, 1993
PubMed

Insights

Oncogenic transformation involves pp60v-src interaction with the cytoskeleton. Platelet activation links pp60c-src to the cytoskeleton via integrins, with tyrosine phosphorylation crucial for platelet function.

Area of Science:

  • Cellular Biology
  • Oncology
  • Biochemistry

Background:

  • Oncogenic transformation mechanisms are incompletely understood.
  • The role of Src family kinases in cellular processes is critical.
  • Proto-oncogene products like pp60c-src are involved in cell signaling.

Purpose of the Study:

  • Investigate the association of pp60v-src with the cytoskeleton during oncogenic transformation.
  • Elucidate the role of pp60c-src in platelet activation and function.
  • Determine the relationship between tyrosine phosphorylation and cellular events.

Main Methods:

  • Utilized various mutants of pp60v-src to study cytoskeleton association.
  • Performed biochemical analysis of fibronectin receptor, vinculin, and talin phosphorylation.
  • Investigated pp60c-src localization and function in activated platelets.

Main Results:

  • pp60v-src interaction with the cytoskeleton, particularly adhesion plaques, correlates with transformation.
  • Tyrosine phosphorylation of the fibronectin receptor is linked to fibronectin loss.
  • Platelet activation causes pp60c-src association with the cytoskeleton, dependent on integrin gpIIb/IIIa occupancy.
  • Tyrosine phosphorylation inhibition impairs integrin-dependent platelet aggregation and signaling.

Conclusions:

  • pp60v-src's cytoskeletal association is a key mechanism in oncogenic transformation.
  • pp60c-src plays a vital role in platelet activation through integrin signaling.
  • Tyrosine phosphorylation is essential for linking matrix receptor occupancy to platelet function.

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