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First published online December 9, 2005

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ERKsome dimers

All eukaryotic cells use MAP kinase signalling pathways to respond to extracellular stimuli. A key MAP kinase is ERK1. This moves between the cytoplasm and the nucleus and can be regulated by phosphorylation/dephosphorylation. Now, on p. 5767, Rada Philipova and Michael Whitaker report that ERK1 dimerizes in vitro and in vivo, and that bisphosphodimers (dimers containing two phosphorylated ERK1 molecules) are the most active form of ERK1. By using biochemical techniques and antibodies that recognize different forms of ERK1, the authors show, for example, that ERK1 monophosphodimers (which contain one phosphorylated and one unphosphorylated ERK1 molecule) provide basal MAP kinase activity in sea urchin eggs. Phosphorylated ERK1 monomers contribute little to ERK1 activity in vivo, whereas peak kinase activity results from the accumulation of bisphosphodimers. From these and other results, the authors suggest that it may be energetically and kinetically efficient for cells to maintain a pool of low-activity ERK1 dimers that can be activated by a single phosphorylation step.

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Related articles in JCS:

Active ERK1 is dimerized in vivo: bisphosphodimers generate peak kinase activity and monophosphodimers maintain basal ERK1 activity

Rada Philipova and Michael Whitaker
JCS 2005 118: 5767-5776. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?