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Association of Src-Related Kinase Lyn with the Interleukin-2 Receptor and Its Role in Maintaining Constitutive Phosphorylation of JAK/STAT in Human T-Cell Leukemia Virus Type 1-Transformed T Cells

  1. Author:
    Shuh, M. S. M.
    Morse, B. A.
    Heidecker, G.
    Derse, D.

  2. Author Address

    [Shuh, M Shuh, M] Xavier Univ, Div Basic Pharmaceut Sci, Coll Pharm, New Orleans, LA 70125 USA [Morse, BA] Centocor Ortho Biotech Inc, Horsham, PA 19044 USA [Heidecker, G; Derse, D] NCI, HIV Drug Resistance Program, Retrovirus Gene Regulat Sect, Frederick, MD 21702 USA;Shuh, M (reprint author), Xavier Univ, Div Basic Pharmaceut Sci, Coll Pharm, 1 Drexel Dr, New Orleans, LA 70125 USA
    1. Year: 2011
    2. Date: May
  2. Journal: Journal of Virology
    1. 85
    2. 9
    3. Pages: 4623-4627
  4. Type of Article: Article
  5. ISSN: 0022-538X
  1. Abstract:

    Human T-cell leukemia virus type 1 (HTLV-1) infection and transformation are associated with an incremental switch in the expression of the Src-related protein tyrosine kinases Lck and Lyn. We examined the physical and functional interactions of Lyn with receptors and signal transduction proteins in HTLV-1-infected T cells. Lyn coimmunoprecipitates with the interleukin-2 beta receptor (IL-2R beta) and JAK3 proteins; however, the association of Lyn with the IL-2R beta and Lyn kinase activity was independent of IL-2 stimulation. Phosphorylation of Janus kinase 3 (JAK3) and signal transducers and activator of transcription 5 (STAT5) proteins was reduced by treatment of cells with the Src kinase inhibitor PP2 or by ectopic expression of a dominant negative Lyn kinase protein.

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External Sources

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  2. DOI: 10.1128/jvi.00839-10
  3. View record in Web of Science®
  4. WOS: 000289618600058

Library Notes

  1. Fiscal Year: FY2010-2011
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