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Science 11 January 1991:
Vol. 251. no. 4990, pp. 192 - 194
DOI: 10.1126/science.1702903
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Articles

Science, Vol 251, Issue 4990, 192-194
Copyright © 1991 by American Association for the Advancement of Science

articles

Association of B cell antigen receptor with protein tyrosine kinase Lyn

Y Yamanashi, T Kakiuchi, J Mizuguchi, T Yamamoto, and K Toyoshima

Department of Oncology, University of Tokyo, Japan.

Antigen is thought to cross-link membrane-bound immunoglobulins (Igs) of B cells, causing proliferation and differentiation or the inhibition of growth. Protein tyrosine kinases are probably involved in signal transduction for cell proliferation and differentiation. The Src-like protein tyrosine kinase Lyn is expressed preferentially in B cells. The Lyn protein and its kinase activity could be coimmunoprecipitated with IgM from detergent lysates. Cross-linking of membrane-bound IgM induced a rapid increase in tyrosine phosphorylation of at least ten distinct proteins of B cells. Thus, Lyn is physically associated with membrane-bound IgM, and is suggested to participate in antigen-mediated signal transduction.


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Regulation of the Adapter Molecule Grb2 by the Fc[IMAGE]R1 in the Mast Cell Line RBL2H3.
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Tyrosine phosphorylation of CD22 during B cell activation.
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M. Clark, K. Campbell, A Kazlauskas, S. Johnson, M Hertz, T. Potter, C Pleiman, and J. Cambier (1992)
Science 258, 123-126
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Tyrosine Phosphorylation of the vav Proto-Oncogene Product in Activated B Cells.
X. R. Bustelo and M. Barbacid (1992)
Science 256, 1196-1199
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Regulation of B cell antigen receptor signal transduction and phosphorylation by CD45.
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Science 252, 1839-1842
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Science 252, 1523-1528
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