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Cross‐linking of the B cell receptor induces activation of phospholipase D through Syk, Btk and phospholipase C‐γ2
Author(s) -
Hitomi Tomohiro,
Yanagi Shigeru,
Inatome Ryoko,
Yamamura Hirohei
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00153-2
Subject(s) - syk , bruton's tyrosine kinase , lyn , phospholipase d , b cell receptor , breakpoint cluster region , signal transduction , microbiology and biotechnology , phospholipase c , chemistry , cancer research , tyrosine kinase , receptor , biology , b cell , biochemistry , immunology , antibody
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.