Dimerization in MAP-kinase signaling

Research output: Contribution to journalArticle

135 Citations (Scopus)

Abstract

The stimulus-dependent nuclear localization of the extracellular-signal- regulated kinases ERK1 and ERK2 is required for many of their actions, including induction of neurites in PC12 cells and transformation of fibroblasts. Phosphorylation of ERK2 causes it to form dimers, and the most flexible portions of the ERK2 molecule provide the surfaces for dimerization. It is thought that dimerization promotes nuclear localization of ERK2 by its effects on import, export or retention in cytoplasmic and nuclear compartments. Dimerization might also influence substrate interactions. Copyright (C) 2000 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)7-9
Number of pages3
JournalTrends in Biochemical Sciences
Volume25
Issue number1
DOIs
StatePublished - Jan 1 2000

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Dimerization
Phosphotransferases
Nuclear Localization Signals
Phosphorylation
PC12 Cells
Extracellular Signal-Regulated MAP Kinases
Neurites
Fibroblasts
Dimers
Molecules
Substrates

ASJC Scopus subject areas

  • Biochemistry

Cite this

Dimerization in MAP-kinase signaling. / Cobb, Melanie H.; Goldsmith, Elizabeth J.

In: Trends in Biochemical Sciences, Vol. 25, No. 1, 01.01.2000, p. 7-9.

Research output: Contribution to journalArticle

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