Related resources
Full-text held externally
- PMID: 18374651
- UKPMCID: 18374651
- DOI: 10.1016/j.molcel.2008.01.019
Search for item elsewhere
University researcher(s)
Academic department(s)
MAP kinase-mediated c-fos regulation relies on a histone acetylation relay switch.
O'Donnell, Amanda; Yang, Shen-Hsi; Sharrocks, Andrew D
Molecular cell. 2008;29(6):780-5.
Access to files
Full-text and supplementary files are not available from Manchester eScholar. Full-text is available externally using the following links:
Full-text held externally
- PMID: 18374651
- UKPMCID: 18374651
- DOI: 10.1016/j.molcel.2008.01.019
Abstract
Gene activation is often associated with high levels of histone acetylation. Enhanced acetylation levels can promote the recruitment of further chromatin modifying complexes or the basal transcription machinery. Here, we have studied MAP kinase-mediated upregulation of c-fos and uncover a role for histone acetylation in promoting the recruitment of a second transcription factor, NFI. MAP kinase signaling to Elk-1 enhances the net histone acetylase activity associated with the c-fos promoter, which leads to changes in the acetylation state and structure of a promoter-proximal nucleosome, which allows NFI binding. Binding of NFI provides a permissive state for the recruitment of basal machinery and subsequent promoter activation. Our results provide insights into how MAP kinase signaling promotes inducible gene expression; phosphorylation of recipient transcription factors (primary effectors) triggers a HAT relay switch, which facilitates the recruitment of additional transcription factors (secondary effectors) through alteration of the local nucleosomal structure.