Monomeric and dimeric models of ERK2 in conjunction with studies on cellular localization, nuclear translocation, and in vitro analysis

Mol Cells. 2012 Apr;33(4):325-34. doi: 10.1007/s10059-012-0023-4. Epub 2012 Mar 23.


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 responses 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 experimental 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Nucleus / metabolism
  • Cytoplasm / metabolism
  • Gene Expression Regulation*
  • Humans
  • MAP Kinase Signaling System* / genetics
  • Mitogen-Activated Protein Kinase 1* / chemistry
  • Mitogen-Activated Protein Kinase 1* / genetics
  • Mitogen-Activated Protein Kinase 1* / metabolism
  • Phosphorylation
  • Protein Multimerization*
  • Protein Transport
  • Signal Transduction*


  • MAPK1 protein, human
  • Mitogen-Activated Protein Kinase 1