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Sci. Signal., 19 June 2012
Vol. 5, Issue 229, p. pc13
[DOI: 10.1126/scisignal.2003287]

PODCASTS

Science Signaling Podcast: 19 June 2012

Holly A. Ingraham1, Raymond D. Blind1, and Annalisa M. VanHook2

1 Department of Cellular and Molecular Pharmacology, Mission Bay Campus, University of California San Francisco, San Francisco, California 94158, USA.
2 Web Editor, Science Signaling, American Association for the Advancement of Science, 1200 New York Avenue, NW, Washington, DC 20005, USA.

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.

Citation: H. A. Ingraham, R. D. Blind, A. M. VanHook, Science Signaling Podcast: 19 June 2012. Sci. Signal. 5, pc13 (2012).

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