14-3-3Gamma interacts with and is phosphorylated by multiple protein kinase C isoforms in PDGF-stimulated human

M V Autieri1, C J Carbone

  • 1Department of Cardiology and Physiology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA. mautieri@unix.temple.edu

DNA and Cell Biology
|August 5, 1999
PubMed

Insights

Growth factors like platelet-derived growth factor (PDGF) regulate 14-3-3gamma protein expression and phosphorylation in vascular smooth muscle cells (VSMC). Protein kinase C (PKC) pathways are involved in this growth factor-induced signaling.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Protein Biochemistry

Background:

  • The 14-3-3 protein family is crucial for signal transduction pathways regulating cellular proliferation.
  • 14-3-3gamma expression is induced by growth factors in human vascular smooth muscle cells (VSMC).

Purpose of the Study:

  • To investigate the role of 14-3-3gamma in growth factor-mediated signal transduction in VSMC.
  • To elucidate the post-translational modifications and regulatory mechanisms of 14-3-3gamma.

Main Methods:

  • Cloning of human 14-3-3gamma.
  • Analysis of 14-3-3gamma expression and phosphorylation in PDGF-treated VSMC.
  • Inhibition studies using protein kinase C (PKC) inhibitors and activators.
  • Co-immunoprecipitation assays to identify interacting proteins.

Main Results:

  • Platelet-derived growth factor (PDGF) induces 14-3-3gamma expression and phosphorylation in VSMC.
  • PKC activation is essential for PDGF-induced 14-3-3gamma phosphorylation.
  • 14-3-3gamma interacts with multiple PKC isoforms and the signal transduction protein Raf-1.

Conclusions:

  • 14-3-3gamma is a signal transduction protein regulated transcriptionally and post-translationally by growth factors.
  • PKC pathways mediate PDGF-induced 14-3-3gamma phosphorylation, linking growth factor signaling to downstream effectors like Raf-1.

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