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J Biol Chem, Vol. 274, Issue 31, 21900-21907, July 30, 1999
From the Instituto de Investigaciones Citológicas, Amadeo de
Saboya 4, 46010 Valencia, Spain
ERK1 and ERK2 associate with the tyrosine
phosphatase PTP-SL through a kinase interaction motif (KIM) located in
the juxtamembrane region of PTP-SL. A glutathione
S-transferase (GST)-PTP-SL fusion protein containing the
KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with
the related JNK1 kinase or with protein kinase A or C. Accordingly,
ERK2 showed in vitro substrate specificity to phosphorylate
GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine
dephosphorylation of ERK2 by the PTP-SL
Interaction of Mitogen-activated Protein Kinases with the Kinase
Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate
Specificity and Retains ERK2 in the Cytoplasm
KIM mutant was impaired. The
in vitro association of ERK1/2 with GST-PTP-SL was highly
stable; however, low concentrations of nucleotides partially
dissociated the ERK1/2·PTP-SL complex. Partial deletions of the KIM
abrogated the association of PTP-SL with ERK1/2, indicating that KIM
integrity is required for interaction. Amino acid substitution analysis
revealed that Arg and Leu residues within the KIM are essential for the
interaction and suggested a regulatory role for Ser231.
Finally, coexpression of PTP-SL and ERK2 in COS-7 cells resulted in the
retention of ERK2 in the cytoplasm in a KIM-dependent
manner. Our results demonstrate that the noncatalytic region of PTP-SL associates with mitogen-activated protein kinases with high affinity and specificity, providing a mechanism for substrate specificity, and
suggest a role for PTP-SL in the regulation of mitogen-activated protein kinase translocation to the nucleus upon activation.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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