Evidence map›Paper›PMID 31061093›Full record

ArticleMolecular and cellular biology2019

GP78 Cooperates with Dual-Specificity Phosphatase 1 To Stimulate Epidermal Growth Factor Receptor-Mediated Extracellular Signal-Regulated Kinase Signaling.

Dhong Hyo Kho, Mohammed Hafiz Uddin, Madhumita Chatterjee, Andreas Vogt, Avraham Raz, Gen Sheng Wu

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

11 citing papers in PubMed, 14 citations in OpenAlex.

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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

6 authors at 3 institutions in 1 country.

Dhong Hyo KhoDepartments of Oncology and Pathology, Karmanos Cancer Institute, Wayne State University School of Medicine, Detroit, Michigan, USA.
Mohammed Hafiz UddinDepartments of Oncology and Pathology, Karmanos Cancer Institute, Wayne State University School of Medicine, Detroit, Michigan, USA.
Madhumita ChatterjeeDepartments of Oncology and Pathology, Karmanos Cancer Institute, Wayne State University School of Medicine, Detroit, Michigan, USA.
Andreas VogtDepartment of Computational and Systems Biology, Drug Discovery Institute, University of Pittsburgh, Pittsburgh, Pennsylvania, USA.
Avraham RazDepartments of Oncology and Pathology, Karmanos Cancer Institute, Wayne State University School of Medicine, Detroit, Michigan, USA.
Gen Sheng WuDepartments of Oncology and Pathology, Karmanos Cancer Institute, Wayne State University School of Medicine, Detroit, Michigan, USA wug@karmanos.org.
Wayne State University · USThe Barbara Ann Karmanos Cancer Institute · USUniversity of Pittsburgh · US

Funding

Developing targeted therapies for triple-negative breast cancerR01CA174949 · NCI · WAYNE STATE UNIVERSITY · PI WU, GEN SHENG · 2014 to 2020
$1.4M
NCI NIH HHS R01 CA174949
6 · The paper itself

Abstract

GP78 is an autocrine motility factor (AMF) receptor (AMFR) with E3 ubiquitin ligase activity that plays a significant role in tumor cell proliferation, motility, and metastasis. Aberrant extracellular signal-regulated kinase (ERK) activation via receptor tyrosine kinases promotes tumor proliferation and invasion. The activation of GP78 leads to ERK activation, but its underlying mechanism is not fully understood. Here, we show that GP78 is required for epidermal growth factor receptor (EGFR)-mediated ERK activation. On one hand, GP78 interacts with and promotes the ubiquitination and subsequent degradation of dual-specificity phosphatase 1 (DUSP1), an endogenous negative regulator of mitogen-activated protein kinases (MAPKs), resulting in ERK activation. On the other hand, GP78 maintains the activation status of EGFR, as evidenced by the fact that EGF fails to induce EGFR phosphorylation in GP78-deficient cells. By the regulation of both EGFR and ERK activation, GP78 promotes cell proliferation, motility, and invasion. Therefore, this study identifies a previously unknown signaling pathway by which GP78 stimulates ERK activation via DUSP1 degradation to mediate EGFR-dependent cancer cell proliferation and invasion.

Indexed as

Carcinoma, HepatocellularCell Line, TumorCell MovementCell ProliferationDual Specificity Phosphatase 1Epidermal Growth FactorErbB ReceptorsHEK293 CellsHumansLiver NeoplasmsMAP Kinase Signaling SystemNeoplasm InvasivenessPhosphorylationProteolysisReceptors, Autocrine Motility FactorUbiquitinationAMFR protein, humanDual Specificity Phosphatase 1DUSP1 protein, humanEGFR protein, humanEpidermal Growth FactorErbB ReceptorsReceptors, Autocrine Motility FactorDUSP1EGFRERKGP78ubiquitination

Identifiers

PMID31061093
PMCPMC6517599
OpenAlexW2942547153

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.