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In vivo association between p56lck and MAP kinase during IL-2-mediated lymphocyte proliferation

J Taieb1, D A Blanchard, M T Auffredou

  • 1INSERM U131, Clamart, France.

Journal of Immunology (Baltimore, Md. : 1950)
|December 15, 1995
PubMed

Insights

p56lck protein associates with MAP kinase during the S phase of the cell cycle, controlling DNA synthesis in B and T lymphocytes stimulated by IL-2.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • p56lck expression increases in B lymphocytes after mitogenic stimulation.
  • Investigating molecular interactions of p56lck in B cells is crucial for understanding lymphocyte activation.

Purpose of the Study:

  • To identify molecules associated with p56lck in vivo.
  • To determine the role of p56lck-MAP kinase association in IL-2-mediated DNA synthesis.

Main Methods:

  • Immunoprecipitation of p56lck from leukemic B cells.
  • In vitro kinase assays and cell cycle analysis.
  • Stimulation with anti-mu antibody and IL-2.

Main Results:

  • p56lck associates with the IL-2 receptor beta chain and p42 MAP kinase.
  • p56lck-associated MAP kinase undergoes phosphorylation, indicating activation.
  • This association occurs specifically during the S phase of the cell cycle and is linked to DNA synthesis.

Conclusions:

  • p56lck and MAP kinase form a complex during S phase.
  • This complex is directly involved in regulating IL-2-driven DNA synthesis in both B and T lymphocytes.

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