Startseite Structure and function of MK5/PRAK: the loner among the mitogen-activated protein kinase-activated protein kinases
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Structure and function of MK5/PRAK: the loner among the mitogen-activated protein kinase-activated protein kinases

  • Ugo Moens

    Ugo Moens obtained his MSc at the University of Ghent, Belgium. He started working on poliovirus at the Free University of Brussels, Belgium. He moved to the University of Tromsø, Norway, where he started working on the human polyomavirus BK. He obtained his PhD in 1992. Currently, he is a professor and division head of the Molecular Inflammation Research Group. His research interests are mitogen-activated protein kinase signaling pathways and human polyomaviruses.

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    und Sergiy Kostenko

    Sergiy Kostenko obtained his MSc degree at the Odessa I.I. Mechnikov State University, Ukraine. He investigated the benzodiazepine functional differentiation in Bogatskiy PhysicoChemical Institute (Odessa, Ukraine) and the reinforcement effect of Hippocampal Early Long-Term Potentiation (LTP) in freely moving animals in Leibniz Institute for Neurobiology (Magdeburg, Germany). He worked on the MAPKAP kinase 5 at the University of Tromsø where he obtained his PhD in 2009 and continued his research as a postdoc. Currently, he is doing his second postdoc in cellular signaling and bioenergetics at the Department of Molecular Biology, University of Bergen, Norway.

Veröffentlicht/Copyright: 29. Mai 2013

Abstract

Mitogen-activated protein kinase (MAPK) pathways are important signal transduction pathways that control pivotal cellular processes including proliferation, differentiation, survival, apoptosis, gene regulation, and motility. MAPK pathways consist of a relay of consecutive phosphorylation events exerted by MAPK kinase kinases, MAPK kinases, and MAPKs. Conventional MAPKs are characterized by a conserved Thr-X-Tyr motif in the activation loop of the kinase domain, while atypical MAPKs lack this motif and do not seem to be organized into the classical three-tiered kinase cascade. One functional group of conventional and atypical MAPK substrates consists of protein kinases known as MAPK-activated protein kinases. Eleven mammalian MAPK-activated protein kinases have been identified, and they are divided into five subgroups: the ribosomal-S6-kinases RSK1-4, the MAPK-interacting kinases MNK1 and 2, the mitogen- and stress-activated kinases MSK1 and 2, the MAPK-activated protein kinases MK2 and 3, and the MAPK-activated protein kinase MK5 (also referred to as PRAK). MK5/PRAK is the only MAPK-activated protein kinase that is a substrate for both conventional and atypical MAPK, while all other MAPKAPKs are exclusively phosphorylated by conventional MAPKs. This review focuses on the structure, activation, substrates, functions, and possible implications of MK5/PRAK in malignant and nonmalignant diseases.


Corresponding author: Ugo Moens, University of Tromsø, Faculty of Health Sciences, Department of Medical Biology, Molecular Inflammation Research Group, N-9037 Tromsø, Norway

About the authors

Ugo Moens

Ugo Moens obtained his MSc at the University of Ghent, Belgium. He started working on poliovirus at the Free University of Brussels, Belgium. He moved to the University of Tromsø, Norway, where he started working on the human polyomavirus BK. He obtained his PhD in 1992. Currently, he is a professor and division head of the Molecular Inflammation Research Group. His research interests are mitogen-activated protein kinase signaling pathways and human polyomaviruses.

Sergiy Kostenko

Sergiy Kostenko obtained his MSc degree at the Odessa I.I. Mechnikov State University, Ukraine. He investigated the benzodiazepine functional differentiation in Bogatskiy PhysicoChemical Institute (Odessa, Ukraine) and the reinforcement effect of Hippocampal Early Long-Term Potentiation (LTP) in freely moving animals in Leibniz Institute for Neurobiology (Magdeburg, Germany). He worked on the MAPKAP kinase 5 at the University of Tromsø where he obtained his PhD in 2009 and continued his research as a postdoc. Currently, he is doing his second postdoc in cellular signaling and bioenergetics at the Department of Molecular Biology, University of Bergen, Norway.

Research in our laboratory is supported by the Mohn Foundation (Tromsø Forskningsstiftelse), Helse-Nord, and the Norwegian Cancer Society. The authors thank Roy Lyså for preparing Figures 1 and 5.

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Received: 2013-3-15
Accepted: 2013-5-28
Published Online: 2013-05-29
Published in Print: 2013-09-01

©2013 by Walter de Gruyter Berlin Boston

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