Evidence map›Paper›PMID 32952126›Full record

ReviewThe Journal of biological chemistry2020

A structural view of PA2G4 isoforms with opposing functions in cancer.

Brendan W Stevenson, Michael A Gorman, Jessica Koach, Belamy B Cheung, Glenn M Marshall, Michael W Parker, Jessica K Holien

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.0field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 45 citations in OpenAlex.

  1. MUC13-Associated Molecular Interactome in Pancreatic Cancer.Computational and structural biotechnology journal · 2026
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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

7 authors at 4 institutions in 2 countries.

Brendan W StevensonSt. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Michael A GormanBio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Jessica KoachDepartment of Pediatrics, Helen Diller Family Comprehensive Cancer Center, University of California, San Francisco, California, USA; Children's Cancer Institute Australia for Medical Research, Lowy Cancer Research Centre, University of New South Wales, Sydney, New South Wales, Australia.
Belamy B CheungChildren's Cancer Institute Australia for Medical Research, Lowy Cancer Research Centre, University of New South Wales, Sydney, New South Wales, Australia; School of Women's and Children's Health, University of New South Wales, Randwick, New South Wales, Australia.
Glenn M MarshallSchool of Women's and Children's Health, University of New South Wales, Randwick, New South Wales, Australia; Kids Cancer Centre, Sydney Children's Hospital, Randwick, New South Wales, Australia.
Michael W ParkerSt. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Jessica K HolienSt. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia; Department of Surgery, University of Melbourne, Parkville, Victoria, Australia; School of Science, College of Science, Engineering, and Health, RMIT University, Melbourne, Victoria, Australia. Electronic address: jessica.holien@rmit.edu.au.
University of Melbourne · AUChildren's Cancer Institute Australia · AUSt Vincents Institute of Medical Research · AUUNSW Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role of proliferation-associated protein 2G4 (PA2G4), alternatively known as ErbB3-binding protein 1 (EBP1), in cancer has become apparent over the past 20 years. PA2G4 expression levels are correlated with prognosis in a range of human cancers, including neuroblastoma, cervical, brain, breast, prostate, pancreatic, hepatocellular, and other tumors. There are two PA2G4 isoforms, PA2G4-p42 and PA2G4-p48, and although both isoforms of PA2G4 regulate cellular growth and differentiation, these isoforms often have opposing roles depending on the context. Therefore, PA2G4 can function either as a contextual tumor suppressor or as an oncogene, depending on the tissue being studied. However, it is unclear how distinct structural features of the two PA2G4 isoforms translate into different functional outcomes. In this review, we examine published structures to identify important structural and functional components of PA2G4 and consider how they may explain its crucial role in the malignant phenotype. We will highlight the lysine-rich regions, protein-protein interaction sites, and post-translational modifications of the two PA2G4 isoforms and relate these to the functional cellular role of PA2G4. These data will enable a better understanding of the function and structure relationship of the two PA2G4 isoforms and highlight the care that will need to be undertaken for those who wish to conduct isoform-specific structure-based drug design campaigns.

Indexed as

Adaptor Proteins, Signal TransducingHumansNeoplasm ProteinsNeoplasmsProtein IsoformsRNA-Binding ProteinsStructure-Activity RelationshipAdaptor Proteins, Signal TransducingNeoplasm ProteinsPA2G4 protein, humanProtein IsoformsRNA-Binding Proteinscancercancer biologydrug targetErbB3-binding protein 1 (EBP1)proliferation-associated protein 2G4 (PA2G4)protein targetingreceptor structure-functionstructure-function

Identifiers

PMID32952126
PMCPMC7681029
OpenAlexW3087715923

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.