You are currently viewing the abstract.
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.
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.
Abstract
This Podcast features an interview with Holly Ingraham and Raymond Blind, authors of a Research Article published in the 19 June 2012 issue of Science Signaling. Ingraham and Blind discuss their discovery of an unusual mechanism by which the activity of the nuclear receptor steroidogenic factor 1 (SF-1) is modulated. The phospholipid phosphatidylinositol bisphosphate (PIP2) binds to SF-1 so that its hydrophilic head group is exposed. A nuclear lipid kinase phosphorylates PIP2 to form PIP3 while it is bound to SF-1. Whereas the SF-1–PIP2 complex cannot bind to DNA, the SF-1–PIP3 complex binds to the promoters of target genes. It is well established that chemical modification of ligands can affect the activity of the receptors to which they are bound, but the mechanism reported in this paper is unusual in that the ligand is chemically modified while bound to the receptor.