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Tyrosine phosphorylation of CRKL in Philadelphia+ leukemia
J ten Hoeve, RB Arlinghaus, JQ Guo, N Heisterkamp and J Groffen
Department of Pathology, Childrens Hospital of Los Angeles.
The chimeric BCR/ABL protein is characteristic of Philadelphia (Ph)+
leukemia because it is the direct product of the Ph translocation and it
has been shown to play a causal role in the genesis of leukemia. The
BCR/ABL protein exhibits a deregulated tyrosine-kinase activity capable of
phosphorylating different cellular substrates in vivo and in vitro. CRKL,
an adaptor protein consisting of SH2 and SH3 domains in the absence of a
catalytic domain, is one potential in vivo substrate of BCR/ABL. Previous
experiments have shown that CRKL is phosphorylated on tyrosine in the
chronic myelogenous leukemia (CML) cell line K562 and that CRKL is a
substrate for ABL and for BCR/ABL in COS-1 cells. In the current study, we
show that in peripheral blood cells a direct correlation exists between the
presence of BCR/ABL and the phosphorylation status of CRKL. In Ph-
peripheral blood cells, CRKL is present only in the nonphosphorylated form.
In contrast, all BCR/ABL+ CML and acute lymphoblastic leukemia patient
samples examined showed clear tyrosine-phosphorylation of CRKL. This result
strongly suggests that CRKL is a biologically significant substrate for
BCR/ABL and is likely to play a major role in the development of Ph+
leukemia.
Volume 84,
Issue 6,
pp. 1731-1736,
09/15/1994
Copyright © 1994 by The American Society of Hematology
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