Catalytic Activation of the Phosphatase MKP-3 by ERK2 Mitogen-Activated Protein Kinase by Montserrat Camps, Anthony Nichols, Corine Gillieron, Bruno Antonsson,

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Catalytic Activation of the Phosphatase MKP-3 by ERK2 Mitogen-Activated Protein Kinase by Montserrat Camps, Anthony Nichols, Corine Gillieron, Bruno Antonsson, Marco Muda, Christian Chabert, Ursula Boschert, and Steve Arkinstall Science Volume 280(5367):1262-1265 May 22, 1998 ©1998 by American Association for the Advancement of Science

Figure 1 Activation of MKP-3 by ERK2. Activation of MKP-3 by ERK2. Phosphatase activity was measured as p-NPP hydrolysis at 25°C monitored at an absorbance of 405 nm (A405) (10). Full-length GST–MKP-3 and GST-ERK2 were expressed inE. coli and purified on glutathione-Sepharose. ERK2 was further purified by ion-exchange chromatography (9,10). (A) Time-dependent hydrolysis ofp-NPP by 5 μg of GST–MKP-3 either alone (0 μg) or in the presence of the indicated amounts of ERK2. Linear reaction rates are indicated by lines of best fit. Ten micrograms of ERK2 stimulated phosphatase activity by 25.5-fold. (B) Activation of the indicated amounts of GST–MKP-3 by purified ERK2. Incubations were for 30 min. Maximal ERK2-dependent activation with 10 μg of MKP-3 was 35 times the basal phosphatase activity. Data points are the mean of duplicate determinations and are representative of three independent experiments. Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Figure 2 Requirement of the MKP-3 catalytic Cys-293 and binding to the MKP-3 NH2-terminus for ERK2-dependent activation. Requirement of the MKP-3 catalytic Cys-293 and binding to the MKP-3 NH2-terminus for ERK2-dependent activation. Phosphatase activity was measured as described (Fig. 1). Incubations were performed with the indicated concentrations of (A) WT GST–MKP-3, (B) inactive mutant GST–MKP-3 C293S, or (C) NH2-terminally truncated GST–MKP-3ΔN (amino acids 153 to 381) in the absence (○) or presence (•) of ERK2 (5 μg). (D) Inhibition of ERK2-dependent activation of MKP-3 by the indicated concentrations of mutant inactive GST–MKP-3 (C293S) (▿), the MKP-3 NH2-terminus GST-MKP-3ΔC (amino acids 1 to 221) (•), or GST protein (○) incubated in the presence of GST–MKP-3 (2.5 μg) and ERK2 (2.5 μg). (▪) MKP-3 activity in the absence of ERK2. Data represent the mean of two identical experiments each performed in triplicate. Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Figure 5 Resistance of ERK2 D319N Sevenmaker to inactivation by MKP-3. Resistance of ERK2 D319N Sevenmaker to inactivation by MKP-3. Wild-type ERK2 (A and C) or ERK2 D319N (B) (0.5 μg) were incubated in vitro in the absence (lane 1) or presence (all other lanes) of 0.1 μg of constitutively active MEK1 (S217E S221E) (16) and with the indicated concentrations (0.01 to 10 μg) of full-length MKP-3 (A and B) or MKP-3ΔN (amino acids 153 to 381) (C). Figure shows autoradiograms of MBP phosphorylation by activated MAP kinases. Experiments were repeated three times with identical results. Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science

Montserrat Camps et al. Science 1998;280:1262-1265 ©1998 by American Association for the Advancement of Science