These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain.
    Author: Marais R, Wynne J, Treisman R.
    Journal: Cell; 1993 Apr 23; 73(2):381-93. PubMed ID: 8386592.
    Abstract:
    The Elk-1 and SRF transcription factors form a ternary complex at the c-fos serum response element (SRE). Growth factor stimulation rapidly induces a reversible change in the electrophoretic mobility of the ternary complex, accompanied by increased phosphorylation of the Elk-1 C-terminal region and by the activation of a 42 kd cellular Elk-1 kinase. Phosphorylation of Elk-1 in vitro by partially purified p42/p44 MAP kinase induces a similar reduction in ternary complex mobility but has little effect on the efficiency of its formation. In vitro, MAP kinase phosphorylates the Elk-1 C-terminal region at multiple sites, which are also phosphorylated following growth factor stimulation in vivo. The Elk-1 C-terminal region functions as a regulated transcriptional activation domain whose activity in vivo is dependent on the integrity of the MAP kinase sites. These findings directly link transcriptional activation by the SRE to the growth factor-regulated phosphorylation of an SRE-binding protein.
    [Abstract] [Full Text] [Related] [New Search]