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TitleStructural mechanism for noncanonical GPCR signaling in the Hedgehog pathway.
Journal, issue, pagesNat Struct Mol Biol, Vol. 33, Issue 5, Page 795-809, Year 2026
Publish dateApr 30, 2026
AuthorsWilliam P Steiner / Nathan Iverson / Guibing Liu / Varun Venkatakrishnan / Jian Wu / Tomasz Maciej Stepniewski / Zachary Michaelson / Jan W Bröckel / Ju-Fen Zhu / Jessica G H Bruystens / Annabel Lee / Isaac Nelson / Daniela Bertinetti / Corvin D Arveseth / Gerald Tan / Paul Spaltenstein / Jiewei Xu / Ruth Hüttenhain / Michael S Kay / Friedrich W Herberg / Erhu Cao / Jana Selent / Ganesh S Anand / Roland L Dunbrack / Susan S Taylor / Benjamin R Myers /
PubMed AbstractThe Hedgehog (Hh) pathway is fundamental to embryogenesis, tissue homeostasis and cancer. Hh signals are transduced through an unusual mechanism; upon agonist-induced phosphorylation, the ...The Hedgehog (Hh) pathway is fundamental to embryogenesis, tissue homeostasis and cancer. Hh signals are transduced through an unusual mechanism; upon agonist-induced phosphorylation, the noncanonical G-protein-coupled receptor (GPCR) Smoothened (SMO) binds the protein kinase A (PKA) catalytic subunit (PKA-C) and physically blocks its enzymatic activity. Here, by combining computational structural approaches with biochemical and functional studies, we show that SMO mimics strategies prevalent in canonical GPCR and PKA signaling complexes, despite little sequence or secondary-structure homology. The intrinsically disordered SMO cytoplasmic domain binds the PKA-C active site, resembling the regulatory subunit within PKA holoenzymes, while the SMO transmembrane domain binds a conserved PKA-C interaction hub. Unlike prevailing GPCR signal transduction models, phosphorylation of SMO promotes intramolecular electrostatic interactions that stabilize structural elements within its cytoplasmic domain, thereby remodeling it into a PKA-inhibiting conformation. Our work provides a structural mechanism for a central step in Hh signaling and defines a principle for disordered GPCR domains to transmit signals intracellularly.
External linksNat Struct Mol Biol / PubMed:42062515 / PubMed Central
MethodsEM (single particle)
Resolution5.08 - 8.59 Å
Structure data

EMDB-72508: BS3-crosslinked Smoothened/PKA-C complex
Method: EM (single particle) / Resolution: 8.59 Å

EMDB-74330: SMO/PKA-C complex, mixed prior to grid preparation
Method: EM (single particle) / Resolution: 6.35 Å

EMDB-74331: SMO/PKA-C complex in MSP1E3D1 nanodiscs
Method: EM (single particle) / Resolution: 8.57 Å

EMDB-74332: Disulfide-trapped SMO-L637C/PKA-C complex
Method: EM (single particle) / Resolution: 5.41 Å

EMDB-74333: EDC/Sulfo-NHS-crosslinked SMO/PKA-C complex
Method: EM (single particle) / Resolution: 5.08 Å

EMDB-74334: SMO/PKA-C complex, dual EDC/Sulfo-NHS and BS3 crosslinking
Method: EM (single particle) / Resolution: 5.3 Å

Source
  • Mus musculus (house mouse)
  • Bos taurus (domestic cattle)

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