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J Biol Chem, Vol. 274, Issue 17, 11693-11700, April 23, 1999
From the Division of Cell Biology, La Jolla Institute for Allergy
and Immunology, San Diego, California 92121
Activation of T lymphocytes to produce cytokines
is regulated by the counterbalance of protein-tyrosine kinases and
protein-tyrosine phosphatases, many of which have a high degree of
substrate specificity because of physical association with their
targets. Overexpression of hematopoietic protein-tyrosine phosphatase
(HePTP) results in suppression of T lymphocyte activation as measured
by T cell antigen receptor-induced activation of transcription factors
binding to the 5' promoter of the interleukin-2 gene. Efforts to
pinpoint the exact site of action and specificity of HePTP in the
signaling cascade revealed that HePTP acts directly on the
mitogen-activated protein (MAP) kinases Erk1 and 2 and consequently
reduces the magnitude and duration of their catalytic activation in
intact T cells. In contrast, HePTP had no effects on N-terminal c-Jun kinase or on events upstream of the MAP kinases. The specificity of
HePTP correlated with its physical association through its noncatalytic
N terminus with Erk and another MAP kinase, p38, but not Jnk or other
proteins. We propose that HePTP plays a negative role in antigen
receptor signaling by specifically regulating MAP kinases in the
cytosol and at early time points of T cell activation before the
activation-induced expression of nuclear dual-specific MAP kinase phosphatases.
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