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Related Experiment Videos

Integrin-dependent PLC-gamma1 phosphorylation mediates fibronectin-dependent adhesion.

Denis Tvorogov1, Xue-Jie Wang, Roy Zent

  • 1Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.

Journal of Cell Science
|January 20, 2005
PubMed
Summary

Phospholipase C-gamma1 (PLC-gamma1) is crucial for efficient cell adhesion to fibronectin, with its Src kinase-dependent phosphorylation at Tyr783 being essential for this process.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Integrin engagement triggers signaling pathways like focal-adhesion kinase (FAK) and Src kinase activation.
  • The specific role of phosphoinositide turnover in cell adhesion remains less understood.

Purpose of the Study:

  • To investigate the function of Phospholipase C-gamma1 (PLC-gamma1) in cell adhesion.
  • To elucidate the molecular mechanisms underlying PLC-gamma1's role in integrin-mediated signaling.

Main Methods:

  • Comparison of Plcg1(-/-) fibroblasts (Null) with re-expressed PLC-gamma1 (Null+).
  • Assessment of cell adhesion rates on fibronectin at varying concentrations.
  • Analysis of integrin subunit expression, receptor clustering, and tyrosine phosphorylation sites (Tyr783, Tyr771, Tyr1253) using site-specific antibodies and mutants.

Related Experiment Videos

  • Inhibition studies using Src-kinase and epidermal-growth-factor-receptor kinase inhibitors.
  • Co-immunoprecipitation assays to determine protein interactions.

    • Main Results:

    • Null cells showed significantly impaired adhesion to fibronectin, particularly at low concentrations.
    • PLC-gamma1 tyrosine phosphorylation at Tyr783 was essential for fibronectin-dependent adhesion; mutagenesis of this site abrogated adhesion.
    • The SH2 domains of PLC-gamma1 were required for maximal adhesion.
    • Fibronectin-induced PLC-gamma1 tyrosine phosphorylation was dependent on Src kinase activity and occurred in a FAK-independent manner.
    • PLC-gamma1 directly associated with Src kinase following fibronectin-induced integrin activation.

    Conclusions:

    • Phospholipase C-gamma1 plays a critical role in regulating cell adhesion to fibronectin.
    • Src kinase-mediated phosphorylation of PLC-gamma1 at Tyr783 is a key event for integrin-dependent adhesion.
    • PLC-gamma1 functions downstream or independently of FAK in this adhesion pathway, highlighting a novel signaling mechanism involving Src kinase.