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Mol. Cells 2012; 33(4): 325-334

Published online March 23, 2012

https://doi.org/10.1007/s10059-012-0023-4

© The Korean Society for Molecular and Cellular Biology

Monomeric and Dimeric Models of ERK2 in Conjunction with Studies on Cellular Localization, Nuclear Translocation, and In Vitro Analysis

Sunbae Lee*, and Yun Soo Bae

Division of Life Sciences, Center for Cell Signal.ing Research, Ewha Womans University, Seoul 120-750, Korea

Correspondence to : *Correspondence: sunblee@ewha.ac.kr

Received: January 19, 2012; Revised: February 21, 2012; Accepted: February 27, 2012

Abstract

Extracellular signal-regulated protein kinase 2 (ERK2) plays many vital roles in cellular signal regulation. Phosphorylation of ERK2 leads to propagation and execution of various extracellular stimuli, which influence cellular respon-ses to stress. The final response of the ERK2 signaling pathway is determined by localization and duration of active ERK2 at specific target cell compartments through protein-protein interactions of ERK2 with various cytoplasmic and nuclear substrates, scaffold proteins, and anchoring counterparts. In this respect, dimerization of phosphorylated ERK2 has been suggested to be a part of crucial regulating mechanism in various protein-protein interactions. After the report of putative dimeric structure of active ERK2 (Canagarajah et al., 1997), dimeric model was employed to explain many in vivo and in vitro experi-mental results. But more recently, many reports have been presented questioning the validity of dimer hypothesis of active ERK2. In this review, we summarize the various in vitro and in vivo studies concerning the Monomeric or the dimeric forms of ERK2 and the validity of the dimer hypothesis.

Keywords ERK2, MAP kinase, nuclear translocation, phosphorylation, scaffold protein

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Mol. Cells 2012; 33(4): 325-334

Published online April 30, 2012 https://doi.org/10.1007/s10059-012-0023-4

Copyright © The Korean Society for Molecular and Cellular Biology.

Monomeric and Dimeric Models of ERK2 in Conjunction with Studies on Cellular Localization, Nuclear Translocation, and In Vitro Analysis

Sunbae Lee*, and Yun Soo Bae

Division of Life Sciences, Center for Cell Signal.ing Research, Ewha Womans University, Seoul 120-750, Korea

Correspondence to:*Correspondence: sunblee@ewha.ac.kr

Received: January 19, 2012; Revised: February 21, 2012; Accepted: February 27, 2012

Abstract

Extracellular signal-regulated protein kinase 2 (ERK2) plays many vital roles in cellular signal regulation. Phosphorylation of ERK2 leads to propagation and execution of various extracellular stimuli, which influence cellular respon-ses to stress. The final response of the ERK2 signaling pathway is determined by localization and duration of active ERK2 at specific target cell compartments through protein-protein interactions of ERK2 with various cytoplasmic and nuclear substrates, scaffold proteins, and anchoring counterparts. In this respect, dimerization of phosphorylated ERK2 has been suggested to be a part of crucial regulating mechanism in various protein-protein interactions. After the report of putative dimeric structure of active ERK2 (Canagarajah et al., 1997), dimeric model was employed to explain many in vivo and in vitro experi-mental results. But more recently, many reports have been presented questioning the validity of dimer hypothesis of active ERK2. In this review, we summarize the various in vitro and in vivo studies concerning the Monomeric or the dimeric forms of ERK2 and the validity of the dimer hypothesis.

Keywords: ERK2, MAP kinase, nuclear translocation, phosphorylation, scaffold protein

Mol. Cells
May 31, 2023 Vol.46 No.5, pp. 259~328
COVER PICTURE
The alpha-helices in the lamin filaments are depicted as coils, with different subdomains distinguished by various colors. Coil 1a is represented by magenta, coil 1b by yellow, L2 by green, coil 2a by white, coil 2b by brown, stutter by cyan, coil 2c by dark blue, and the lamin Ig-like domain by grey. In the background, cells are displayed, with the cytosol depicted in green and the nucleus in blue (Ahn et al., pp. 309-318).

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