Evidence map›Paper›PMID 27856640›Full record

ArticleThe Journal of biological chemistry2016

G protein-coupled receptors (GPCRs) That Signal via Protein Kinase A (PKA) Cross-talk at Insulin Receptor Substrate 1 (IRS1) to Activate the phosphatidylinositol 3-kinase (PI3K)/AKT Pathway.

Nathan C Law, Morris F White, Mary E Hunzicker-Dunn

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.0field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed, 78 citations in OpenAlex.

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  16. Analysis of the Expression ofCurrent genomics · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Nathan C LawFrom the School of Molecular Biosciences, Washington State University, Pullman, Washington 99164 and.
Morris F Whitethe Division of Endocrinology, Dept. of Medicine, Boston Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115.
Mary E Hunzicker-DunnFrom the School of Molecular Biosciences, Washington State University, Pullman, Washington 99164 and mehd@wsu.edu.
Washington State University · USHarvard University · US

Funding

WOUND HEALINGP50GM021700 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI MARTYN, JEEVENDRA · 1985 to 2017
$27.2M
Regulating IRS-proteins by Ser/Thr PhosphorylationR01DK038712 · NIDDK · JOSLIN DIABETES CENTER · PI WHITE, MORRIS F. · 1992 to 2014
$5.0M
Metabolic Crosstalk During Hepatic Insulin ResistanceR01DK098655 · NIDDK · BOSTON CHILDREN'S HOSPITAL · PI WHITE, MORRIS F. · 2013 to 2020
$4.0M
FSH-Stimulated Signals that Regulate Follicular MaturationR01HD062053 · NICHD · WASHINGTON STATE UNIVERSITY · PI HUNZICKER-DUNN, MARY E, NILSON, JOHN H. · 2009 to 2013
$1.5M
Functional Significance of the HIF1 Transcriptome in Granulosa CellsR01HD065859 · NICHD · WASHINGTON STATE UNIVERSITY · PI HUNZICKER-DUNN, MARY E, NILSON, JOHN H. · 2010 to 2014
$1.5M
Molecular Bioscience Graduate Training ProgramT32GM083864 · NIGMS · WASHINGTON STATE UNIVERSITY · PI NILSON, JOHN H. · 2010 to 2014
$646k
NICHD NIH HHS R01 HD062053NICHD NIH HHS R01 HD065859NIDDK NIH HHS R01 DK038712NIDDK NIH HHS R01 DK098655NIGMS NIH HHS P50 GM021700NIGMS NIH HHS T32 GM083864
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) activate PI3K/v-AKT thymoma viral oncoprotein (AKT) to regulate many cellular functions that promote cell survival, proliferation, and growth. However, the mechanism by which GPCRs activate PI3K/AKT remains poorly understood. We used ovarian preantral granulosa cells (GCs) to elucidate the mechanism by which the GPCR agonist FSH via PKA activates the PI3K/AKT cascade. Insulin-like growth factor 1 (IGF1) is secreted in an autocrine/paracrine manner by GCs and activates the IGF1 receptor (IGF1R) but, in the absence of FSH, fails to stimulate YXXM phosphorylation of IRS1 (insulin receptor substrate 1) required for PI3K/AKT activation. We show that PKA directly phosphorylates the protein phosphatase 1 (PP1) regulatory subunit myosin phosphatase targeting subunit 1 (MYPT1) to activate PP1 associated with the IGF1R-IRS1 complex. Activated PP1 is sufficient to dephosphorylate at least four IRS1 Ser residues, Ser

Indexed as

AnimalsBreast NeoplasmsCells, CulturedCyclic AMP-Dependent Protein KinasesFemaleGranulosa CellsHumansInsulin Receptor Substrate ProteinsOvarian FolliclePhosphatidylinositol 3-KinasePhosphorylationProto-Oncogene Proteins c-aktRatsRats, Sprague-DawleyReceptors, G-Protein-CoupledSignal TransductionCyclic AMP-Dependent Protein KinasesInsulin Receptor Substrate ProteinsPhosphatidylinositol 3-KinaseProto-Oncogene Proteins c-aktReceptors, G-Protein-CoupledG protein-coupled receptor (GPCR)insulin-like growth factor (IGF)insulin receptor substrate 1 (IRS1)PI3KPKA

Identifiers

PMID27856640
PMCPMC5207145
OpenAlexW2567371399

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.