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Direct binding of CRKL to BCR-ABL is not required for BCR-ABL
transformation
C Heaney, K Kolibaba, A Bhat, T Oda, S Ohno, S Fanning and BJ Druker
Division of Hematology and Medical Oncology, Oregon Health Sciences
University, Portland 97201, USA.
CRKL has previously been shown to be a major tyrosine phosphorylated
protein in neutrophils of patients with BCR-ABL+ chronic myelogenous
leukemia and in cell lines expressing BCR-ABL CRKL and BCR-ABL form a
complex as demonstrated by coimmunoprecipitation and are capable of a
direct interaction in a yeast two-hybrid assay. We have mapped the site of
interaction of CRKL and BCR-ABL to the amino terminal SH3 domain of CRKL
with a proline rich region in the C-terminus of ABL. The proline- rich
region was mutated and the effect of this deletion on BCR-ABL transforming
function was assayed. Our data show that this deletion does not impair the
ability of BCR-ABL to render myeloid cells factor independent for growth.
In cells expressing the proline deletion mutation of BCR-ABL, CRKL is still
tyrosine phosphorylated and forms a complex with BCR-ABL as demonstrated by
coimmunoprecipitation. Our data suggest that the interaction between CRKL
and the proline deletion mutant of BCR-ABL is an indirect interaction as
CRKL does not interact directly with the proline deletion mutant of BCR-ABL
in a gel overlay assay or in a yeast two-hybrid assay. Thus, a direct
interaction of CRKL and BCR-ABL is not required for CRKL to become tyrosine
phosphorylated by BCR-ABL and suggests that CRKL function may still be
required for BCR-ABL function through an indirect interaction.
Volume 89,
Issue 1,
pp. 297-306,
01/01/1997
Copyright © 1997 by The American Society of Hematology
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