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Genomic organization of the Shc-related phosphotyrosine adapters and characterization of the full-length Sck/ShcB: Specific association of p68-Sck/ShcB with pp135

  1. Author:
    Kojima, T.
    Yoshikawa, Y.
    Takada, S.
    Sato, M.
    Nakamura, T.
    Takahashi, N.
    Copeland, N. G.
    Gilbert, D. J.
    Jenkins, N. A.
    Mori, N.

  2. Author Address

    Natl Inst Longev Sci, Dept Mol Genet, Morioka, Aichi 4748522, Japan. NILS, Dept Mol Genet Res, Morioka, Aichi 4748522, Japan. NAIST, Dept Biosci, Takayama, Nara 6300101, Japan. Kyoto Univ, Fac Sci, Ctr Dev Biol, Kyoto 6068224, Japan. NCI, Frederick Canc Res & Dev Ctr, ABL Basic Res Program, Mammalian Genet Lab, Ft Detrick, MD 21702 USA. Mori N Natl Inst Longev Sci, Dept Mol Genet, Morioka, Aichi 4748522, Japan.
    1. Year: 2001
  2. Journal: Biochemical and Biophysical Research Communications
    1. 284
    2. 4
    3. Pages: 1039-1047
  4. Type of Article: Article
  1. Abstract:

    The She gene family is an emerging family, containing at least three members designated Shc/ShcA, Sck/Sli/ShcB, N-Shc/Rai/ShcC in mammals. In this study, we determined the genomic organization of the mouse She family. Coding regions of ShcA, B, and C each comprised 12 exons, spanned approximately 6, 20, and 65 kb, and located on chromosome 3, 10, and 13, respectively. Based on this genome analysis, we determined the full-length structure of mouse Sck/ShcB as a 68-kD protein. We found that the 68-kD full-length Sck/ShcB was more efficiently phosphorylated upon EGF treatment than the previously-analyzed CH2-deleted form. We also found that Sck specifically interacted with a 135-kD phosphoprotein (pp135) through its SH2 domain following membrane depolarization. The Sck-pp135 interaction was reduced by Src kinase inhibitors. These results suggest that Sck, but not N-Shc nor She, transmit signals in conjunction with pp135 following Src activation and/or calcium entry in the cell. (C) 2001 Academic Press.

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