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Volume 272, Number 29,
Issue of July 18, 1997
pp. 18200-18208
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Syk Is Required for BCR-mediated Activation of p90Rsk, but Not
p70S6k, via a Mitogen-activated Protein Kinase-independent Pathway in B
Cells
(Received for publication, March 27, 1997, and in revised form, May 7, 1997)
Hsiu-Ling
Li
,
Mark S.
Forman
,
Tomohiro
Kurosaki
and
Ellen
Puré
From the Wistar Institute, Philadelphia, Pennsylvania 19104 and the
Department of Molecular Genetics, Institute for Hepatic
Research, Kansai Medical University, Moriguchi 570, Japan
The tyrosine kinases Syk and Lyn are activated in
B lymphocytes following antibody induced cross-linking of the B cell
receptor for antigen (BCR). It has been suggested that activation of
Syk is dependent on Lyn. We tested this hypothesis by comparing the phosphorylation and activation of several downstream effector molecules
in parental DT40, DT40Syk and DT40Lyn
B cells. The phosphorylation and activation of p90Rsk was ablated in
Syk-deficient B cells but unaffected in Lyn-deficient B cells while the
phosphorylation/activation of Ras GTPase activating protein (Ras GAP)
and mitogen activated protein (MAP) kinase required both Syk and Lyn.
Thus, these data indicate that Syk can be activated in the absence of
Lyn after BCR cross-linking and results in the activation of p90Rsk via
a MAP kinase-independent pathway in DT40Lyn cells. We
also demonstrated that BCR mediates the activation of p70S6k. However,
activation of p70S6k in DT40Syk and DT40Lyn
cells was comparable with that observed in parental cells. Thus, either
Syk or Lyn may be sufficient for activation of p70S6k, or activation of
p70S6k occurs independently of both Syk and Lyn. The kinase activity of
Syk was required for the phosphorylation/activation of each of these
downstream effector molecules but only the phosphorylation of Ras GAP
was affected in cells expressing a mutant of Syk in which tyrosines 525 and 526 were substituted to phenlyalanines.

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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.
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