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Association of Src‐Family Kinase Lyn with B‐Cell Antigen Receptor
Author(s) -
Yamamoto Tadashi,
Yamanashi Yuji,
Toyoshima Kumao
Publication year - 1993
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1111/j.1600-065x.1993.tb00843.x
Subject(s) - lyn , medical science , library science , medicine , biology , kinase , proto oncogene tyrosine protein kinase src , genetics , computer science , medical education
Antigen is thought to cross-link membrane-bound immunoglobulins (Igs) of B cells, causing proliferation and differentiation or the inhibition of growth. Compelling evidence suggests that protein-tyrosine phosphorylation is involved in signal transduction for cell proliferation and differentiation. Indeed cross-linking of membrane-bound IgM (mIgM) induced a rapid increase in tyrosine phosphorylation of at least 10 distinct proteins in B cells. The Src-family protein tyrosine kinase Lyn (p56lyn and p53lyn) is expressed preferentially in B cells. The Lyn protein and its kinase activity could be coimmunoprecipitated with both IgM and IgD from detergent lysates. Cross-linking of membrane-bound IgM with antibody induced down-regulation of the Lyn protein. From these data we concluded that Lyn is physically associated with mIgs. Further evidence showed that cross-linking of mIgM induced rapid increase in the kinase activity of Lyn and association of Lyn with 85-kDa noncatalytic subunit of phosphatidylinositol 3-kinase. Thus, Lyn is likely to participate in B-cell antigen receptor-mediated signaling. As a novel signaling molecule downstream of Lyn, we identified src homology 3-containing, transcription factor-like molecule p75HS1.