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J Biol Chem, Vol. 274, Issue 38, 26697-26704, September 17, 1999
From the Departments of Neurology and Neurosciences and the
Alzheimer Research Laboratory, Case Western Reserve University School
of Medicine, Cleveland, Ohio 44106
The protein-tyrosine phosphatase PTP-1B is an
important regulator of intracellular protein tyrosine phosphorylation,
and is itself regulated by phosphorylation. We report that PTP-1B and its yeast analog, YPTP, are phosphorylated and activated by members of
the CLK family of dual specificity kinases. CLK1 and CLK2
phosphorylation of PTP-1B in vitro activated the
phosphatase activity approximately 3-5-fold using either
p-nitrophenol phosphate, or tyrosine-phosphorylated myelin
basic protein as substrates. Co-expression of CLK1 or CLK2 with PTP-1B
in HEK 293 cells led to a 2-fold stimulation of phosphatase activity
in vivo. Phosphorylation of PTP-1B at Ser50 by
CLK1 or CLK2 is responsible for its enzymatic activation. These
findings suggest that phosphorylation at Ser50 by serine
threonine kinases may regulate the activation of PTP-1B in
vivo. We also show that CLK1 and CLK2 phosphorylate and activate the S. cerevisiae PTP-1B family member, YPTP1. CLK1
phosphorylation of YPTP1 led to a 3-fold stimulation of phosphatase
activity in vitro. We demonstrate that CLK phosphorylation
of Ser83 on YPTP1 is responsible for the activation of this
enzyme. These findings demonstrate that the CLK kinases activate PTP-1B
family members, and this phosphatase may be an important cellular
target for CLK action.
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