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Tyrosine phosphorylation of rasGAP and associated proteins in chronic
myelogenous leukemia cell lines
B Druker, K Okuda, U Matulonis, R Salgia, T Roberts and JD Griffin
Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA
02115.
The Philadelphia chromosome (Ph1), detected in virtually all cases of
chronic myelogenous leukemia, is formed by a reciprocal translocation
between chromosomes 9 and 22 that fuses BCR encoded sequences upstream of
exon 2 of c-ABL. This oncogene produces a fusion protein (p210BCR/ABL) in
which the ABL tyrosine kinase activity is elevated. This elevated kinase
activity is essential for transformation, but the mechanisms involved are
unknown. We report here that p21ras GTPase activating protein (rasGAP) or
rasGAP-associated proteins p190 and p62 are phosphorylated on tyrosine in
Ph1 (+) cell lines. Further, rasGAP coimmunoprecipitates with p210BCR/ABL
in these cell lines. These results suggest that rasGAP or associated
proteins are potential substrates for p210BCR/ABL kinase and thus directly
link p210BCR/ABL with a signal transduction pathway known to be activated
by hematopoietic growth factors (p21ras).
Volume 79,
Issue 9,
pp. 2215-2220,
05/01/1992
Copyright © 1992 by The American Society of Hematology
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