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Related Experiment Video

Updated: Jul 4, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Does MK5 reconcile classical and atypical MAP kinases?

Maria Perander¹, Stephen M Keyse, Ole-Morten Seternes

¹Department of Pharmacology, Institute of Medical Biology, University of Tromso, N-9037 Tromso, Norway.

Frontiers in Bioscience : a Journal and Virtual Library

|May 30, 2008

Summary

MAP kinase-activated protein kinase 5 (MK5) is not activated by cellular stress like other related kinases. Instead, MK5 appears to be regulated by atypical MAP kinases ERK3 and ERK4, suggesting a distinct signaling role.

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Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

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Published on: June 30, 2019

Area of Science:

Cellular signaling pathways
Protein kinase regulation
MAP kinase family

Background:

MAP kinase-activated protein kinase 5 (MK5), also known as PRAK, was initially identified as downstream of p38 MAP kinase.
MK5 shares sequence similarity with MK2 and MK3, which are activated by cellular stress and inflammatory cytokines.
However, MK5 does not exhibit activation in response to these stimuli.

Purpose of the Study:

To investigate the distinct activation and physiological function of MK5 compared to other MAPKAP kinases.
To explore the signaling pathways that regulate MK5 activity.
To understand the role of MK5 in cellular stress and inflammatory responses.

Main Methods:

Analysis of MK5 activation in response to cellular stress and inflammatory stimuli.
Phenotypic analysis of MK5-deficient (null) mice, including response to endotoxic shock and LPS-induced cytokine expression.
Investigation of MK5 complex formation with atypical MAP kinases ERK3 and ERK4.

Main Results:

MK5-deficient mice show normal responses to endotoxic shock and unchanged cytokine expression upon LPS challenge, unlike MK2/MK3 deficient mice.
MK5 is not activated by cellular stress or pro-inflammatory cytokines, despite its sequence similarity to MK2/MK3.
MK5 is uniquely regulated and activated through complex formation with atypical MAP kinases ERK3 and ERK4.

Conclusions:

MK5 functions distinctly from MK2 and MK3, as it is not activated by classical stress pathways.
MK5's unique regulation by ERK3 and ERK4 suggests it operates downstream of alternative signaling cascades.
This finding positions MK5 as a unique member of the MAPKAP kinase family with a potentially novel physiological role.