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Interferon α activates the tyrosine kinase Lyn in haemopoietic cells
Author(s) -
Uddin Shahab,
Grumbach Isabella M.,
YI Taolin,
Colamonici Oscar R.,
Platanias Leonidas C.
Publication year - 1998
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1046/j.1365-2141.1998.00731.x
Subject(s) - lyn , proto oncogene tyrosine protein kinase src , tyrosine kinase , sh2 domain , cancer research , sh3 domain , microbiology and biotechnology , tyrosine protein kinase csk , biology , janus kinase , src family kinase , kinase , signal transduction , chemistry
We investigated whether the src‐family tyrosine kinase Lyn is involved in the generation of interferon α (IFNα) signals in haemopoietic cells. In vitro kinase assays using IFNα‐sensitive cells of B‐cell origin demonstrated the presence of IFNα‐dependent kinase activity in anti‐Lyn immunoprecipitates. Further studies demonstrated that Lyn associates via its src homology 2 (SH2) domain with the Janus family tyrosine kinase Tyk‐2. This interaction was IFNα‐dependent and involved direct binding of the SH2 domain of Lyn to the IFNα‐activated form of Tyk‐2. Thus, during binding of IFNα to its receptor in malignant haemopoietic cells, Lyn is engaged in an IFNα‐signalling pathway, probably downstream of Tyk‐2.