Evidence map›Paper›PMID 25113560›Full record

ArticleMolecular and cellular biology2014

Plakophilin-2 promotes tumor development by enhancing ligand-dependent and -independent epidermal growth factor receptor dimerization and activation.

Kei-ichiro Arimoto, Christoph Burkart, Ming Yan, Dan Ran, Stephanie Weng, Dong-Er Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

31 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
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  5. TRPML3/BK complex promotes autophagy and bacterial clearance by providing a positive feedback regulation of mTOR via PI3P.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
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  9. Review
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  13. Article
  14. Desmosomes as Signaling Hubs in the Regulation of Cell Behavior.Frontiers in cell and developmental biology · 2021
    Review
  15. Article
  16. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Kei-ichiro ArimotoMoores UCSD Cancer Center, University of California, San Diego, La Jolla, California, USA karimoto@ucsd.edu d7zhang@ucsd.edu.
Christoph BurkartMoores UCSD Cancer Center, University of California, San Diego, La Jolla, California, USA.
Ming YanMoores UCSD Cancer Center, University of California, San Diego, La Jolla, California, USA.
Dan RanMoores UCSD Cancer Center, University of California, San Diego, La Jolla, California, USA.
Stephanie WengMoores UCSD Cancer Center, University of California, San Diego, La Jolla, California, USA.
Dong-Er ZhangMoores UCSD Cancer Center, University of California, San Diego, La Jolla, California, USA Department of Pathology and Division of Biological Sciences, University of California, San Diego, La Jolla, California, USA karimoto@ucsd.edu d7zhang@ucsd.edu.
University of California San Diego · USUniversity of San Diego · US

Funding

VIRAL MALIGNANCYP30CA023100 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DIANE M SIMEONE · 1985 to 2026
$124.9M
ISG15 and Protein ISGylation in CancerR01CA177305 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ZHANG, DONG-ER · 2013 to 2023
$3.7M
UBP43 in HematopoiesisR01HL091549 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ZHANG, DONG-ER · 2008 to 2012
$1.9M
NCI NIH HHS P30 CA023100NCI NIH HHS R01 CA177305NCI NIH HHS R01CA177305NHLBI NIH HHS R01 HL091549NHLBI NIH HHS R01HL091549
6 · The paper itself

Abstract

Epidermal growth factor (EGF) receptor (EGFR) has been implicated in tumor development and invasion. Dimerization and autophosphorylation of EGFR are the critical events for EGFR activation. However, the regulation of EGF-dependent and EGF-independent dimerization and phosphorylation of EGFR has not been fully understood. Here, we report that cytoplasmic protein plakophilin-2 (PKP2) is a novel positive regulator of EGFR signaling. PKP2 specifically interacts with EGFR via its N-terminal head domain. Increased PKP2 expression enhances EGF-dependent and EGF-independent EGFR dimerization and phosphorylation. Moreover, PKP2 knockdown reduces EGFR phosphorylation and attenuates EGFR-mediated signal activation, resulting in a significant decrease in proliferation and migration of cancer cells and tumor development. Our results indicate that PKP2 is a novel activator of the EGFR signaling pathway and a potential new drug target for inhibiting tumor growth.

Indexed as

AnimalsCarcinogenesisCell Line, TumorCell MovementCell ProliferationEpidermal Growth FactorErb-b2 Receptor Tyrosine KinasesErbB ReceptorsFemaleHEK293 CellsHumansLigandsMammary Neoplasms, ExperimentalMiceMice, Inbred NODMice, SCIDEGFR protein, humanEpidermal Growth FactorERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesErbB ReceptorsLigandsPKP2 protein, humanPlakophilins

Identifiers

PMID25113560
PMCPMC4187709
OpenAlexW1975337963

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.