Different domains of the mitogen-activated protein kinases ERK3 and ERK2 direct subcellular localization and upstream specificity in vivo

Megan J. Robinson, Bing e. Xu, Stephen Stippec, Melanie H. Cobb

Research output: Contribution to journalArticle

15 Scopus citations


Extracellular signal-regulated kinase 3 (ERK3) is a member of the mitogen-activated protein (MAP) kinase family. ERK3 is most similar in its kinase catalytic domain to ERK2, yet it displays many unique properties. Among these, unlike ERK2, which translocates to the nucleus following activation, ERK3 is constitutively localized to the nucleus, despite the lack of a defined nuclear localization sequence. We created two chimeras between ERK2 and the catalytic domain of ERK3 (ERK3ΔC), and some mutants of these chimeras, to examine the basis for the different behaviors of these two MAP kinase family members. We find the following: 1) the N-terminal folding domain of ERK3 functions in phosphoryl transfer reactions with the C-terminal folding domain of ERK2; 2) the C-terminal halves of ERK2 and ERK3ΔC are primarily responsible for their subcellular localization in resting cells; and 3) the N-terminal folding domain of ERK2 is required for its activation in cells, its interaction with MEK1, and its accumulation in the nucleus.

Original languageEnglish (US)
Pages (from-to)5094-5100
Number of pages7
JournalJournal of Biological Chemistry
Issue number7
StatePublished - Feb 15 2002


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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