Cross‐linking of the B cell receptor induces activation of phospholipase D through Syk, Btk and phospholipase C‐γ2

FEBS Letters

Hitomi, Tomohiro¹  Yamamura, Hirohei¹  Yanagi, Shigeru¹  Inatome, Ryoko¹ 

[1] Department of Biochemistry, Kobe University School of Medicine, Chuo-ku, Kobe 650-0017, Japan

关键词: B cell receptor;    Phospholipase D;    Syk;    Btk;    Phospholipase C-γ;    Src family;    BCR;    B cell receptor;    PTK;    protein tyrosine kinase;    PIP2;    phosphatidylinositol 4;    5-bisphosphate;    PLC;    phospholipase C;    IP3;    inositol 1;    4;    5-trisphosphate;    DG;    diacylglycerol;    PKC;    protein kinase C;    PLD;    phospholipase D;    PC;    phosphatidylcholine;    PA;    phosphatidic acid;    ARF;    ADP-ribosylation factor;    PEt;    phosphatidylethanol;    FCS;    fetal calf serum;    BIM;    bisindolylmaleimide;    TCR;    T cell receptor;   

DOI  :  10.1016/S0014-5793(99)00153-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phospholipase D (PLD) has been proposed to play a key role in the signal transduction of cellular responses to various extracellular signals. Herein we provide biochemical and genetic evidence that cross-linking of the B cell receptor (BCR) induces rapid activation of PLD through a Syk-, Btk- and phospholipase C (PLC)-γ2-dependent pathway in DT40 cells. Activation of PLD upon BCR engagement is completely blocked in Syk- or Btk-deficient cells, but unaffected in Lyn-deficient cells. Furthermore, in PLC-γ2-deficient cells, BCR engagement failed to activate PLD. These results demonstrate that Syk, Btk and PLC-γ2 are essential for BCR-induced PLD activation.

【 授权许可】

Unknown