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(Received for publication, May 25,
1995; and in revised form, August 11, 1995) To elucidate interactions occurring between B cell protein
tyrosine kinases and the signaling components of the B cell antigen
receptor, we have co-transfected into COS cells individual tyrosine
kinases together with chimeric cell surface receptors containing the
cytoplasmic domains of Ig
Volume 270,
Number 45,
Issue of November 10, 1995 pp. 27072-27078
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
or Ig
. Of the tyrosine kinases
transfected (Lyn, Blk, Hck, Syk, Fyn), only Blk was able to
phosphorylate and subsequently associate with co-transfected Ig
and Ig
chimeras in vivo. Association between Blk and the
Ig
and Ig
cytoplasmic domains was shown by mutational
analyses to be the result of an SH2-phosphotyrosine interaction. We
identified the tyrosine residues of the Ig
and Ig
cytoplasmic
domains phosphorylated by Blk. The enzymatic activity and membrane
association of Blk were required for the observed phosphorylation of
the Ig
and Ig
chimeras. Sequences within the amino-terminal
unique domain of Blk are responsible for recognition and subsequent
phosphorylation of the Ig
chimera since transfer of the unique
region of Blk to Fyn results in the chimeric kinase's ability to
phosphorylate the cytoplasmic domain of Ig
. These findings
indicate that the unique domain of Src family kinases may direct
recognition of certain substrates leading to their phosphorylation.
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