The Bmx Tyrosine Kinase Is Activated by IL-3 and G-CSF in a PI-3K Dependent Manner
Oncogene (2000) 19, 4151 ± 4158 ã 2000 Macmillan Publishers Ltd All rights reserved 0950 ± 9232/00 $15.00 www.nature.com/onc The Bmx tyrosine kinase is activated by IL-3 and G-CSF in a PI-3K dependent manner Niklas Ekman1,6, Elena Arighi1,2,6, Iiro Rajantie1, Pipsa Saharinen3, Ari RistimaÈ ki4, Olli Silvennoinen3,5 and Kari Alitalo*,1 1Molecular/Cancer Biology Laboratory and Ludwig Institute for Cancer Research, Haartman Institute, P.O.Box 21 (Haartmaninkatu 3), 00014 University of Helsinki, Finland; 2Department of Experimental Oncology, Istituto Nazionale Tumori, 20133 Milan, Italy; 3Department of Virology, Haartman Institute, P.O.Box 21 (Haartmaninkatu 3), 00014 University of Helsinki, Finland; 4Department of Obstetrics and Gynecology, Helsinki University Central Hospital, P.O. Box 140, 00029 Helsinki, Finland; 5Medical Biochemistry, University of Tampere, 33014 Tampere, Finland Cytoplasmic protein tyrosine kinases play crucial roles in The Tec family of PTKs consists of ®ve members: the signaling via a variety of cell surface receptors. The Bmx founder member Tec, as well as Btk, Itk/Tsk/Emt, Txk tyrosine kinase, a member of the Tec family, is and Bmx tyrosine kinases. The Tec kinases are regulated expressed in hematopoietic cells of the granulocytic and by a variety of hematopoietic receptors. For example, the monocytic lineages. Here we show that Bmx is Bruton's tyrosine kinase, Btk, is activated through the catalytically activated by interleukin-3 (IL-3) and high anity IgE receptor in mast cells, by the antigen granulocyte-colony stimulating factor (G-CSF) recep- and CD72 receptors in B-cells, as well as by interleukin-3 tors.
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