Sci. Signal., 19 June 2012
Targeting the Lipid Ligand to Regulate TranscriptionSteroidogenic 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.
Citation: R. D. Blind, M. Suzawa, H. A. Ingraham, Direct Modification and Activation of a Nuclear Receptor–PIP2 Complex by the Inositol Lipid Kinase IPMK. Sci. Signal. 5, ra44 (2012).
The editors suggest the following Related Resources on Science sites:
In Science Signaling
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882