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TitleStructure of the phosphoinositide 3-kinase (PI3K) p110γ-p101 complex reveals molecular mechanism of GPCR activation.
Journal, issue, pagesSci Adv, Vol. 7, Issue 35, Year 2021
Publish dateAug 27, 2021
AuthorsManoj K Rathinaswamy / Udit Dalwadi / Kaelin D Fleming / Carson Adams / Jordan T B Stariha / Els Pardon / Minkyung Baek / Oscar Vadas / Frank DiMaio / Jan Steyaert / Scott D Hansen / Calvin K Yip / John E Burke /
PubMed AbstractThe class IB phosphoinositide 3-kinase (PI3K), PI3Kγ, is a master regulator of immune cell function and a promising drug target for both cancer and inflammatory diseases. Critical to PI3Kγ function ...The class IB phosphoinositide 3-kinase (PI3K), PI3Kγ, is a master regulator of immune cell function and a promising drug target for both cancer and inflammatory diseases. Critical to PI3Kγ function is the association of the p110γ catalytic subunit to either a p101 or p84 regulatory subunit, which mediates activation by G protein-coupled receptors. Here, we report the cryo-electron microscopy structure of a heterodimeric PI3Kγ complex, p110γ-p101. This structure reveals a unique assembly of catalytic and regulatory subunits that is distinct from other class I PI3K complexes. p101 mediates activation through its Gβγ-binding domain, recruiting the heterodimer to the membrane and allowing for engagement of a secondary Gβγ-binding site in p110γ. Mutations at the p110γ-p101 and p110γ-adaptor binding domain interfaces enhanced Gβγ activation. A nanobody that specifically binds to the p101-Gβγ interface blocks activation, providing a novel tool to study and target p110γ-p101-specific signaling events in vivo.
External linksSci Adv / PubMed:34452907 / PubMed Central
MethodsEM (single particle)
Resolution3.36 Å
Structure data

EMDB-23812:
Structure of the apo phosphoinositide 3-kinase p110 gamma (PIK3CG) p101 (PIK3R5) complex
Method: EM (single particle) / Resolution: 3.36 Å

Source
  • Homo sapiens (human)

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