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This research aims to elucidate the mechanism by which ERK activates MKP3, a key phosphatase in mitogenic signaling.

Mechanistic Basis for Catalytic Activation of Mitogen-activated Protein Kinase Phosphatase 3 by Extracellular Signal-regulated Kinase

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This research aims to elucidate the mechanism by which ERK activates MKP3, a key phosphatase in mitogenic signaling.
Conducted biochemical assays to analyze the activation mechanism of MKP3 by ERK.
Utilized Brönsted analyses and both pre-steady-state and steady-state kinetics.
Isolated all catalytic steps in the reaction and quantified specific rate enhancements.
Activated MKP3 catalyzes formation of the phosphoenzyme intermediate 100-fold faster than the unactivated form.
ERK-activated MKP3 demonstrates 5-6-fold greater efficiency in hydrolysis and binds ligands 19-fold more tightly.
Chemical chaperone dimethyl sulfoxide mimics ERK activation, stabilizing MKP3's active conformation.

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Biochemical evidence reveals how ERK enhances phosphatase activity in MKP3, suggesting regulatory mechanisms.

Fjeld et al. (2000) studied this question.

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