Article

Defining how oncogenic and developmental mutations of <i>PIK3R1</i> alter the regulation of class IA phosphoinositide 3-kinases

2019-07-16

Abstract excerpt

<h4>Summary</h4> The class IA PI3Ks are key signalling enzymes composed of a heterodimer of a p110 catalytic subunit and a p85 regulatory subunit, with PI3K mutations being causative of multiple human diseases including cancer, primary immunodeficiencies, and developmental disorders. Mutations in the p85α regulatory subunit encoded by PIK3R1 can both activate PI3K through oncogenic truncations in the iSH2 domain...

Topics

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

Identifiers and source

Literature Corpus work: 8e7237c9-3b80-5c90-b3b3-a26d0a81a1ed
DOI: 10.1101/704106

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Defining how oncogenic and developmental mutations of <i>PIK3R1</i> alter the regulation of class IA phosphoinositide 3-kinasesDOI 10.1101/704106Read

Defining How Oncogenic and Developmental Mutations of PIK3R1 Alter the Regulation of Class IA Phosphoinositide 3-Kinases.Semantic proximity Read

Oncogenic mutations of PIK3CA lead to increased membrane recruitment driven by reorientation of the ABD, p85 and C-terminus.Semantic proximity Read

Conformational disruption of PI3Kδ regulation by immunodeficiency mutations in PIK3CD and PIK3R1.Semantic proximity Read

Oncogenic mutations mimic and enhance dynamic events in the natural activation of phosphoinositide 3-kinase p110α (PIK3CA).Semantic proximity Read

Activity and Dynamics of p110α are not Differentially Modulated by Regulatory Subunit IsoformsSemantic proximity Read

Molecular Mechanisms of Human Disease Mediated by Oncogenic and Primary Immunodeficiency Mutations in Class IA Phosphoinositide 3-Kinases.Semantic proximity Read

Molecular basis for plasma membrane recruitment of PI4KA by EFR3Semantic proximity Read

Mechanistic investigation of genotype-phenotype correlations in PIK3R1-related diseasesSemantic proximity Read

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

A novel carcinogenic PI3Kα mutation suggesting the role of helical domain in transmitting nSH2 regulatory signals to kinase domainSemantic proximity Read

Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit.Semantic proximity Read

PIK3IP1: structure, aberration, function, and regulation in diseasesSemantic proximity Read