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Tyrosine phosphorylation of P160 BCR by P210 BCR-ABL
D Lu, J Liu, M Campbell, JQ Guo, N Heisterkamp, J Groffen, E Canaani and R Arlinghaus
Department of Molecular Pathology, University of Texas M.D. Anderson Cancer
Center, Houston 77030.
It is well established that the chimeric BCR-ABL gene formed by joining
parts of the BCR and ABL genes plays a key role in the pathogenesis of
Philadelphia (Ph) chromosome-positive leukemias. We report that
simultaneous expression of P210 BCR-ABL and P160 BCR in simian COS-1 cells
yielded stable complexes of these two proteins, and induced phosphorylation
of P160 BCR on tyrosine residues in vivo. Tyrosine phosphorylation of a
deletion mutant encoding 553 amino acids of BCR N- terminal sequences was
also detected when it was coexpressed with P210 BCR-ABL. We propose that
tyrosine phosphorylation of P160 BCR by P210 BCR-ABL and their stable
physical interaction may perturb normal BCR functions and that these
alterations are directly involved in the pathologic processes found in Ph
chromosome-associated leukemias.
Volume 82,
Issue 4,
pp. 1257-1263,
08/15/1993
Copyright © 1993 by The American Society of Hematology
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