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(Received for publication, September 27, 1996)
From the University of Colorado Health Sciences Center, Department
of Pathology, Denver, Colorado 80262
We have demonstrated that a 120-kDa protein,
identified as Cbl, becomes rapidly phosphorylated on tyrosine residues
following stimulation of factor-dependent cells with
interleukin-3 (IL-3). Little or no phosphorylation of Cbl was observed
in the absence of IL-3 stimulation and phosphorylation is maximal by
20-30 min after IL-3 stimulation. Association of Cbl with Grb2 was
noted in unstimulated cells, and the amount of Cbl associated with Grb2 increased following IL-3 stimulation. The p85 subunit of
phosphatidylinositol 3-kinase was constitutively associated with Cbl.
Approximately 10% of the PI kinase activity present in
anti-phosphotyrosine immunoprecipitates was present in anti-Cbl
immunoprecipitates of IL-3-stimulated cells. The constitutive
association of Cbl with Fyn was also observed. Cbl was observed to bind
to bacterial fusion proteins encoding the unique, SH3, and SH2 domains
of Fyn, Hck, and Lyn. The SH2 domain of Fyn alone was able to bind Cbl to nearly the same extent as did the fusion protein encoding the unique, SH3, and SH2 domains. This was not the case for the SH2 domain
of Hck, however, as binding of the Hck fusion protein to Cbl appeared
to require multiple domains. The binding of the fusion proteins to Cbl
occurred regardless of whether Cbl was tyrosine-phosphorylated or not,
and the binding could not be disrupted by the addition of 30 mM free phosphotyrosine. These data suggest the unexpected conclusion that the Fyn SH2 domain may bind to Cbl in a
phosphotyrosine-independent manner.
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