Article

Structure of the phosphoinositide 3-kinase p110γ-p101 complex reveals molecular mechanism of GPCR activation

2021-06-01

Abstract excerpt

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 (GPCRs). Here, we report the cryo-EM structure of a heterodimeric P...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 6fdabbbc-2760-58ee-9669-01dc4ea13b3f
DOI: 10.1101/2021.06.01.446612

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Structure of the phosphoinositide 3-kinase p110γ-p101 complex reveals molecular mechanism of GPCR activationDOI 10.1101/2021.06.01.446612Read

Disease-related mutations in PI3Kγ disrupt regulatory C-terminal dynamics and reveal a path to selective inhibitors.Semantic proximity Read

Disease related mutations in PI3Kγ disrupt regulatory C-terminal dynamics and reveals a path to selective inhibitorsSemantic proximity Read

Assigning functional domains within the p101 regulatory subunit of phosphoinositide 3-kinase gamma.Semantic proximity Read

Function, Regulation and Biological Roles of PI3Kγ VariantsSemantic proximity Read

Cryo-EM structures of cancer-specific helical and kinase domain mutations of PI3Kα.Semantic proximity Read

The structural basis of PI3K cancer mutations: from mechanism to therapy.Semantic proximity Read

Insights into the oncogenic effects of PIK3CA mutations from the structure of p110alpha/p85alpha.Semantic proximity Read

Class IA PI3K regulatory subunits: p110-independent roles and structures.Semantic proximity Read

The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations.Semantic proximity Read

Structural basis for the activation of PLC-γ isozymes by phosphorylation and cancer-associated mutations.Semantic proximity Read

Structure, function and inhibition of the phosphoinositide 3-kinase p110α enzyme.Semantic proximity Read

Receptor tyrosine kinases activate heterotrimeric G proteins via phosphorylation within the interdomain cleft of GαiSemantic proximity Read