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TitleCryo-EM structural elucidation and molecular mechanism of the GPR133-G13 signaling complex.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 777, Page 152165, Year 2025
Publish dateJun 6, 2025
AuthorsXuanyu Pu / Yue-Tong Xi / Meng-Xin Wang / Daolai Zhang / Yu-Qi Ping / Peng Xiao / Jin-Peng Sun /
PubMed AbstractGPR133 is an adhesion-class G protein-coupled receptor (GPCR) that has recently been de-orphanized. Its functions are complex and multifaceted. While GPR133 is primarily recognized for coupling with ...GPR133 is an adhesion-class G protein-coupled receptor (GPCR) that has recently been de-orphanized. Its functions are complex and multifaceted. While GPR133 is primarily recognized for coupling with the Gs subunit to mediate elevated intracellular cAMP levels, its potential engagement with alternative signaling pathways remains poorly characterized. In our experiments, we demonstrated that GPR133 exhibits constitutive self-activation via its Stachel sequence as an adhesion GPCR, enabling activation of downstream G13 signaling. We reconstituted the GPR133-GAIN-miniGα13 complex in vitro and resolved its cryo-electron microscopy structure at a resolution of 3.51 Å. Detailed structural comparisons between the GPR133-GAIN-miniGα13 complex and the previously resolved GPR133-CTF-Gs structure highlighted both conserved and different features. These findings provide critical insights into the signal transduction mechanisms of GPR133 and lay a foundation for targeted therapeutic strategies.
External linksBiochem Biophys Res Commun / PubMed:40570642
MethodsEM (single particle)
Resolution3.51 Å
Structure data

64672

9v0u

EMDB-64672, PDB-9v0u:
GPR133-Gain-miniG13 complex
Method: EM (single particle) / Resolution: 3.51 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / GPCR / G12/G13 / Complex / Stachel

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