You are currently viewing the editor's summary.
View Full TextLog in to view the full text
AAAS login provides access to Science for AAAS members, and access to other journals in the Science family to users who have purchased individual subscriptions.
Register for free to read this article
As a service to the community, this article is available for free. Existing users log in.
More options
Download and print this article for your personal scholarly, research, and educational use.
Buy a single issue of Science for just $15 USD.
Targeting the Lipid Ligand to Regulate Transcription
Steroidogenic factor 1 (SF-1) is a nuclear receptor that transcriptionally activates genes involved in sexual development and reproduction. Blind et al. found that phosphatidylinositol 4,5-bisphosphate (PIP2) bound to SF-1 was phosphorylated by inositol polyphosphate multikinase (IPMK) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). Conversely, the lipid phosphatase PTEN dephosphorylated the SF-1–PIP3 complex. The transcriptional activity of SF-1 was decreased in cells after inhibiting IPMK and increased in cells overexpressing PTEN. Thus, phosphorylation of its associated lipid, rather than the nuclear receptor itself, activates SF-1 and identifies another signaling role for nuclear phosphoinositides.
