Open AccessDeletion of Src Homology 3 Domain Results in Constitutive Activation of Tec Protein‐Tyrosine Kinase
Author(s) -
Yamashita Yoshihiro,
Miyazato Akira,
Ohya Kenichi,
Ikeda Uichi,
Shimada Kazuyuki,
Miura Yasusada,
Ozawa Keiya,
Mano Hiroyuki
Publication year - 1996
Publication title -
japanese journal of cancer research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 141
eISSN - 1349-7006
pISSN - 0910-5050
DOI - 10.1111/j.1349-7006.1996.tb03118.x
Subject(s) - tec , proto oncogene tyrosine protein kinase src , phosphorylation , tyrosine phosphorylation , tyrosine kinase , biology , tyrosine , microbiology and biotechnology , haematopoiesis , cancer research , chemistry , signal transduction , biochemistry , stem cell , ionosphere , physics , astronomy
Tec protein‐tyrosine kinase (PTK) is the prototype of a new subfamily of non‐receptor type PTKs, and is abundantly expressed in hematopoietic tissues. We have revealed that Tec is inducibly tyrosine‐phosphorylated and activated by stimulation with a wide range of cytokines. To get more insight into the signaling mechanism through Tec, we have generated a constitutively active form of Tec PTK. Deletion of the Src homology (SH) 3 domain gave rise to a hyperphosphorylated and activated Tec kinase (TecΔSH3). The activity of TecΔSH3 was confirmed in 293 cells, as well as in cytokine‐dependent hematopoietic cells (BA/F3). TecΔSH3 should be a useful tool to study the in vivo substrates of Tec PTK.