A Novel Membrane Glycoprotein, SHPS-1, That Binds the SH2-Domain-Containing Protein Tyrosine Phosphatase SHP-2 in Response to Mitogens and Cell Adhesion

DOI Web Site Web Site PubMed 被引用文献17件 オープンアクセス
  • Yohsuke Fujioka
    Second Department of Internal Medicine, Kobe University School of Medicine, Chuo-ku, Kobe 650, Japan
  • Takashi Matozaki
    Second Department of Internal Medicine, Kobe University School of Medicine, Chuo-ku, Kobe 650, Japan
  • Tetsuya Noguchi
    Second Department of Internal Medicine, Kobe University School of Medicine, Chuo-ku, Kobe 650, Japan
  • Akihiro Iwamatsu
    Kirin Brewery Co. Ltd. Central Laboratories for Key Technology, Kanazawa-ku, Yokohama, Kanagawa 236, Japan
  • Takuji Yamao
    Second Department of Internal Medicine, Kobe University School of Medicine, Chuo-ku, Kobe 650, Japan
  • Nobuaki Takahashi
    Kirin Brewery Co. Ltd. Central Laboratories for Key Technology, Kanazawa-ku, Yokohama, Kanagawa 236, Japan
  • Masahiro Tsuda
    Second Department of Internal Medicine, Kobe University School of Medicine, Chuo-ku, Kobe 650, Japan
  • Toshiyuki Takada
    Second Department of Internal Medicine, Kobe University School of Medicine, Chuo-ku, Kobe 650, Japan
  • Masato Kasuga
    Second Department of Internal Medicine, Kobe University School of Medicine, Chuo-ku, Kobe 650, Japan

書誌事項

公開日
1996-12-01
権利情報
  • https://journals.asm.org/non-commercial-tdm-license
DOI
  • 10.1128/mcb.16.12.6887
公開者
Informa UK Limited

この論文をさがす

説明

Protein tyrosine phosphatases (PTPases), such as SHP-1 and SHP-2, that contain Src homology 2 (SH2) domains play important roles in growth factor and cytokine signal transduction pathways. A protein of approximately 115 to 120 kDa that interacts with SHP-1 and SHP-2 was purified from v-src-transformed rat fibroblasts (SR-3Y1 cells), and the corresponding cDNA was cloned. The predicted amino acid sequence of the encoded protein, termed SHPS-1 (SHP substrate 1), suggests that it is a glycosylated receptor-like protein with three immunoglobulin-like domains in its extracellular region and four YXX(L/V/I) motifs, potential tyrosine phosphorylation and SH2-domain binding sites, in its cytoplasmic region. Various mitogens, including serum, insulin, and lysophosphatidic acid, or cell adhesion induced tyrosine phosphorylation of SHPS-1 and its subsequent association with SHP-2 in cultured cells. Thus, SHPS-1 may be a direct substrate for both tyrosine kinases, such as the insulin receptor kinase or Src, and a specific docking protein for SH2-domain-containing PTPases. In addition, we suggest that SHPS-1 may be a potential substrate for SHP-2 and may function in both growth factor- and cell adhesion-induced cell signaling.

収録刊行物

被引用文献 (17)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ