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(Received for publication, April 17, 1996, and in revised form, June 18, 1996)
From the Syk and Zap-70 are related protein-tyrosine
kinases implicated in antigen and Fc receptor signaling. While Zap-70
is restricted to T-cells and natural killer cells, Syk accumulates in
B-cells, mast cells, platelets, and immature T-cells. In addition, we
found that an isoform of Syk (SykB), which carries a 23-amino acid
deletion in the ``linker'' region, is prominently expressed in bone
marrow. To better understand the relative impact of Syk, SykB, and
Zap-70 on signal transduction, we compared their intrinsic enzymatic
properties in transiently transfected COS-1 cells and in hemopoietic
cells. Using modified versions of these enzymes bearing a common Myc
epitope at the amino terminus, we determined that the ability of Syk
and SykB to undergo autophosphorylation and to phosphorylate
erythrocyte band 3 in immune complex kinase reactions was at least
100-fold greater than that of Zap-70. Similarly, Syk and SykB, but not
Zap-70, caused prominent tyrosine phosphorylation of
p120c-cbl in COS-1 cells. A similar pattern of
activity was also noted for endogenous Syk and Zap-70 from hemopoietic
cells. To understand the structural basis for these characteristics, we
also created and analyzed a series of chimeras between Syk and Zap-70.
These studies indicated that the catalytic domain of Syk and Zap-70,
but not their SH2 domains, linker region or carboxyl-terminal tail, was
responsible for their respective activity. Taken together, these data
demonstrated that the intrinsic enzymatic activity of Syk and SykB is
superior to that of Zap-70 and that such a distinction relates to
structural variations in the catalytic domain.
Volume 271, Number 37,
Issue of September 13, 1996
pp. 22782-22790
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,¶
and¶''
McGill Cancer Centre and Departments of
¶ Biochemistry, '' Medicine, and
Oncology, McGill University,
Montréal, Canada H3G 1Y6 and the
Departments of Medicine and Oncology,
Montreal General Hospital, Montréal, Canada H3G 1A4
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