Regulation of Class IA PI 3-kinases: C2 domain-iSH2 domain contacts inhibit p85/p110alpha and are disrupted in oncogenic p85 mutants - Wikidata - awgldk - TriplyDB

Regulation of Class IA PI 3-kinases: C2 domain-iSH2 domain contacts inhibit p85/p110alpha and are disrupted in oncogenic p85 mutants

Regulation of Class IA PI 3-kinases: C2 domain-iSH2 domain contacts inhibit p85/p110alpha and are disrupted in oncogenic p85 mutants

http://www.wikidata.org/entity/Q37453427

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A beta version of life: p110β takes center stage FBXL2- and PTPL1-mediated degradation of p110-free p85β regulatory subunit controls the PI(3)K signalling cascade Will kinase inhibitors make it as glioblastoma drugs?Phosphoinositides: tiny lipids with giant impact on cell regulation Structure of Lipid Kinase p110β/p85β Elucidates an Unusual SH2-Domain-Mediated Inhibitory Mechanism Regulation of lipid binding underlies the activation mechanism of class IA PI3-kinases Signaling by the phosphoinositide 3-kinase family in immune cells A testis-specific regulator of complex and hybrid N-glycan synthesis.PI3K and cancer: lessons, challenges and opportunities Cancer-derived mutations in the regulatory subunit p85alpha of phosphoinositide 3-kinase function through the catalytic subunit p110alpha Structural basis of nSH2 regulation and lipid binding in PI3Kα.A biochemical mechanism for the oncogenic potential of the p110beta catalytic subunit of phosphoinositide 3-kinase.Dominant-activating germline mutations in the gene encoding the PI(3)K catalytic subunit p110δ result in T cell senescence and human immunodeficiency Gain-of-function mutations and immunodeficiency: at a loss for proper tuning of lymphocyte signaling.Oncogenic activity of the regulatory subunit p85β of phosphatidylinositol 3-kinase (PI3K)Identification of mutations in distinct regions of p85 alpha in urothelial cancer.Dynamics of the phosphoinositide 3-kinase p110δ interaction with p85α and membranes reveals aspects of regulation distinct from p110α PI3K in cancer: divergent roles of isoforms, modes of activation and therapeutic targeting.High frequency of PIK3R1 and PIK3R2 mutations in endometrial cancer elucidates a novel mechanism for regulation of PTEN protein stability Gambogenic acid alters chemosensitivity of breast cancer cells to Adriamycin Oncogenic mutations weaken the interactions that stabilize the p110α-p85α heterodimer in phosphatidylinositol 3-kinase α.Oncogenic mutations mimic and enhance dynamic events in the natural activation of phosphoinositide 3-kinase p110α (PIK3CA).Phosphatidylinositol-3,4,5-trisphosphate: tool of choice for class I PI 3-kinases.Insulin resistance and diabetes caused by genetic or diet-induced KBTBD2 deficiency in mice.The structural basis of PI3K cancer mutations: from mechanism to therapy.The regulation of class IA PI 3-kinases by inter-subunit interactions.PI3K/AKT signaling pathway and cancer: an updated review.PI3King the right partner: unique interactions and signaling by p110β.Targeting therapeutic liabilities engendered by PIK3R1 mutations for cancer treatment.Neomorphic mutations create therapeutic challenges in cancer.p85α SH2 domain phosphorylation by IKK promotes feedback inhibition of PI3K and Akt in response to cellular starvation.The structure of p85ni in class IA phosphoinositide 3-kinase exhibits interdomain disorder.Potency and pharmacokinetics of broad spectrum and isoform-specific p110γ and δ inhibitors in cancers.Addition of N-terminal peptide sequences activates the oncogenic and signaling potentials of the catalytic subunit p110α of phosphoinositide-3-kinase Domain analysis reveals striking functional differences between the regulatory subunits of phosphatidylinositol 3-kinase (PI3K), p85α and p85β.The p101 subunit of PI3Kγ restores activation by Gβ mutants deficient in stimulating p110γ.Insights into the pathological mechanisms of p85α mutations using a yeast-based phosphatidylinositol 3-kinase model

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Regulation of Class IA PI 3-kinases: C2 domain-iSH2 domain contacts inhibit p85/p110alpha and are disrupted in oncogenic p85 mutants

http://www.wikidata.org/entity/Q37453427

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name

Regulation of Class IA PI 3-ki ...... upted in oncogenic p85 mutants

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Regulation of Class IA PI 3-ki ...... pted in oncogenic p85 mutants.

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type

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Regulation of Class IA PI 3-ki ...... upted in oncogenic p85 mutants

@en

Regulation of Class IA PI 3-ki ...... pted in oncogenic p85 mutants.

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prefLabel

Regulation of Class IA PI 3-ki ...... upted in oncogenic p85 mutants

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Regulation of Class IA PI 3-ki ...... pted in oncogenic p85 mutants.

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Proceedings of the National Academy of Sciences of the United States of America

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Regulation of Class IA PI 3-ki ...... upted in oncogenic p85 mutants

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Bijay S Jaiswal

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Gary J Gerfen

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Haiyan Wu

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Jonathan M Backer

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K Ilker Sen

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Mark E Girvin

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Mirvat El-Sibai

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Rory J Flinn

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S Chandra Shekar

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Somasekar Seshagiri

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P2860

Alternative modes of binding of proteins with tandem SH2 domains

Phosphatidylinositol 3'-kinase is activated by association with IRS-1 during insulin stimulation

Solution structure of the C-terminal SH2 domain of the p85 alpha regulatory subunit of phosphoinositide 3-kinase

Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85

An integrated genomic analysis of human glioblastoma multiforme

Comprehensive genomic characterization defines human glioblastoma genes and core pathways

Crystal structure of the C-terminal SH2 domain of the p85alpha regulatory subunit of phosphoinositide 3-kinase: an SH2 domain mimicking its own substrate

Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit

The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations

Structure of the PI3K SH3 domain and analysis of the SH3 family

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20258-20263

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10.1073/PNAS.0902369106

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48

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106

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38091089

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19915146

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2787125

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