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First published online July 30, 2004
doi: 10.1242/10.1242/jcs.01346
Commentary |
Nuclear Signalling Laboratory, Department of Biochemistry, Oxford University, South Parks Road, Oxford, OX1 3QU, UK
* Author for correspondence (e-mail: louiscm{at}bioch.ox.ac.uk)
Mitogen-activated protein kinase (MAPK) pathways regulate eukaryotic gene expression in response to extracellular stimuli. MAPKs and their downstream kinases phosphorylate transcription factors, co-regulators and chromatin proteins to initiate transcriptional changes. However, the spatial context in which the MAPKs operate in transcription complexes is poorly understood. Recent findings in budding yeast show that MAPKs can form integral components of transcription complexes and have novel structural functions in addition to phosphorylating local substrates. Hog1p MAPK is stably recruited to target promoters by specific transcription factors in response to osmotic stress, and acts as both a structural adaptor and enzymatic activator driving the assembly and activation of the transcription complex. We review the evidence that suggests a similar bifunctional role for MAPKs in mammalian transcription complexes.
Key words: MAP kinase, Transcription complexes, Hog1/p38
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