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

Title
Monomeric and dimeric models of ERK2 in conjunction with studies on cellular localization, nuclear translocation, and in vitro analysis
Authors
Lee S.Bae Y.S.
Ewha Authors
배윤수이선배
SCOPUS Author ID
배윤수scopus
Issue Date
2012
Journal Title
Molecules and Cells
ISSN
1016-8478JCR Link
Citation
vol. 33, no. 4, pp. 325 - 334
Indexed
SCI; SCIE; SCOPUS; KCI WOS scopus
Abstract
Extracellular signal-regulated protein kinase 2 (ERK2) plays many vital roles in cellular signal regulation. Phosphoryla-tion of ERK2 leads to propagation and execution of various extracellular stimuli, which influence cellular responses to stress. The f inal 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 cyto-plasmic 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. © 2012 KSMCB.
DOI
10.1007/s10059-012-0023-4
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자연과학대학 > 생명과학전공 > Journal papers
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