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J. Biol. Chem., Vol. 276, Issue 19, 16491-16500, May 11, 2001
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From the Imperial Cancer Research Fund Molecular Pharmacology Unit,
Biomedical Research Centre, Level 5, Ninewells Hospital,
Dundee DD1 9SY, Scotland, United Kingdom
Mitogen-activated protein (MAP) kinase
phosphatase 1 (MKP-1/CL100) is an inducible nuclear dual specificity
protein phosphatase that can dephosphorylate and inactivate both
mitogen- and stress-activated protein kinases in vitro and
in vivo. However, the molecular mechanism responsible for
the substrate selectivity of MKP-1 is unknown. In addition, it has been
suggested that the signal transducers and activators of transcription 1 (STAT1) transcription factor is a physiological non-MAP kinase
substrate for MKP-1. We have used the yeast two-hybrid assay to
demonstrate that MKP-1 is able to interact selectively with the
extracellular signal-regulated kinase 1/2 (ERK1/2), p38
Distinct Binding Determinants for ERK2/p38
and JNK MAP Kinases
Mediate Catalytic Activation and Substrate Selectivity of MAP Kinase
Phosphatase-1*,
,
, and c-Jun
NH2-terminal kinase (JNK) MAP kinase isoforms. Furthermore,
this binding is accompanied by catalytic activation of recombinant
MKP-1 protein in vitro, and these end points show an
absolute correlation with MKP-1 substrate selectivity in
vivo. In contrast, MKP-1 does not interact with STAT1.
Recombinant STAT1 does not cause catalytic activation of MKP-1; nor
does MKP-1 block tyrosine phosphorylation of STAT1 in vivo.
Both binding and catalytic activation of MKP-1 are abrogated by
mutation of a conserved docking site in ERK2, p38, and JNK1 MAP
kinases. Within MKP-1, MAP kinase binding is mediated by the amino-terminal noncatalytic domain of the protein. However, mutation of
a conserved cluster of positively charged residues within this domain
abolishes the binding and activation of MKP-1 by ERK2 and p38 but
not JNK1, indicating that there are distinct binding determinants for
these MAP kinase isoforms. We conclude that the substrate selectivity
of MKP-1 is determined by specific protein-protein interactions coupled
with catalytic activation of the phosphatase and that these
interactions are restricted to members of the MAP kinase family of enzymes.
*
This work was supported by the Imperial Cancer Research
Fund.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at
http://www.jbc.org) contains a listing of plasmid constructs.
Recipient of a postdoctoral fellowship from the Norwegian Research
Council (project 123686/310).
§
To whom correspondence should be addressed. Tel.: 01382 632622;
Fax: 01382 669993; E-mail: S.Keyse@icrf.icnet.uk.
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