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IL-7 induces tyrosine phosphorylation of clathrin heavy chain

  1. Author:
    Jiang, Q.
    Benbernou, N.
    Chertov, O.
    Khaled, A. R.
    Wooters, J.
    Durum, S. K.
  2. Author Address

    NCI, Mol Immunoregulat Lab, CCR, NIH, Room 31-71,Bldg 560, Frederick, MD 21702 USA NCI, Mol Immunoregulat Lab, CCR, NIH, Frederick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, SAIC, Intramural Res Support Program, Cambridge, MA 02140 USA Durum SK NCI, Mol Immunoregulat Lab, CCR, NIH, Room 31-71,Bldg 560, Frederick, MD 21702 USA
    1. Year: 2004
  1. Journal: Cellular Signalling
    1. 16
    2. 2
    3. Pages: 281-286
  2. Type of Article: Article
  1. Abstract:

    IL-7 induction of protein tyrosine phosphorylation was examined in an IL-7-dependent thymocyte cell line, D1, which was generated from a P53(-/-) mouse. Anti-phosphotyrosine antibody was used both to immunoprecipitate and Western blot, and showed that IL-7 induced tyrosine phosphorylation of a protein with a molecular weight of approximately 200 kDa. The P200 band was purified by reversed-phase high-performance liquid chromatography. Amino acid sequencing by mass spectrometry revealed three peptides identical to rat clathrin heavy chain (CHC) 1 (192 kDa), and this was confirmed by blotting with an anti-clathrin antibody. Stimulation of normal pro-T cells by IL-7 showed an increased tyrosine phosphorylation of clathrin heavy chain. Tyrosine phosphorylation of clathrin heavy chain was strongly induced by IL-7 and to a lesser extent by IL-4, while no effect could be observed with the cytokines IL-2, IL-9 and IL-15, whose receptors share the gamma(c) chain. Phosphorylation of clathrin heavy chain was found to be sensitive to Jak3 inhibitors but not to Src inhibitors. Clathrin is involved in internalization of many receptors, and its phosphorylation by IL-7 stimulation may affect the internalization of the IL-7 receptor. Published by Elsevier Inc.

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