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• W2270582783 endingPage "e1002375" @default.
• W2270582783 startingPage "e1002375" @default.
• W2270582783 abstract "In Hedgehog (Hh) signaling, binding of Hh to the Patched-Interference Hh (Ptc-Ihog) receptor complex relieves Ptc inhibition on Smoothened (Smo). A longstanding question is how Ptc inhibits Smo and how such inhibition is relieved by Hh stimulation. In this study, we found that Hh elevates production of phosphatidylinositol 4-phosphate (PI(4)P). Increased levels of PI(4)P promote, whereas decreased levels of PI(4)P inhibit, Hh signaling activity. We further found that PI(4)P directly binds Smo through an arginine motif, which then triggers Smo phosphorylation and activation. Moreover, we identified the pleckstrin homology (PH) domain of G protein-coupled receptor kinase 2 (Gprk2) as an essential component for enriching PI(4)P and facilitating Smo activation. PI(4)P also binds mouse Smo (mSmo) and promotes its phosphorylation and ciliary accumulation. Finally, Hh treatment increases the interaction between Smo and PI(4)P but decreases the interaction between Ptc and PI(4)P, indicating that, in addition to promoting PI(4)P production, Hh regulates the pool of PI(4)P associated with Ptc and Smo." @default.
• W2270582783 created "2016-06-24" @default.
• W2270582783 creator A5012581113 @default.
• W2270582783 creator A5018267355 @default.
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• W2270582783 creator A5073501391 @default.
• W2270582783 creator A5083251487 @default.
• W2270582783 date "2016-02-10" @default.
• W2270582783 modified "2023-10-14" @default.
• W2270582783 title "PI(4)P Promotes Phosphorylation and Conformational Change of Smoothened through Interaction with Its C-terminal Tail" @default.
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• W2270582783 doi "https://doi.org/10.1371/journal.pbio.1002375" @default.
• W2270582783 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4749301" @default.
• W2270582783 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26863604" @default.
• W2270582783 hasPublicationYear "2016" @default.
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