Evidence map›Paper›PMID 33060621›Full record

ArticleScientific reports2020

Multivalent tumor suppressor adenomatous polyposis coli promotes Axin biomolecular condensate formation and efficient β-catenin degradation.

Tie-Mei Li, Jing Ren, Dylan Husmann, John P Coan, Or Gozani, Katrin F Chua

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

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  12. Superresolution microscopy localizes endogenous Dvl2 to Wnt signaling-responsive biomolecular condensates.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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 2 countries.

Tie-Mei LiDepartment of Medicine, Stanford University School of Medicine, Stanford, CA, 94305, USA. tiemei.li2@gmail.com.
Jing RenMedical Research Council Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.
Dylan HusmannDepartment of Biology, Stanford University, Stanford, CA, 94305, USA.
John P CoanDepartment of Medicine, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Or GozaniDepartment of Biology, Stanford University, Stanford, CA, 94305, USA. ogozani@stanford.edu.
Katrin F ChuaDepartment of Medicine, Stanford University School of Medicine, Stanford, CA, 94305, USA. kfchua@stanford.edu.
Stanford University · USMedical Research Council · GBVA Palo Alto Health Care System · US

Funding

Leveraging innovative technologies in basic and clinical cancer researchT32CA009302 · NCI · STANFORD UNIVERSITY · PI LAURA D ATTARDI, Aaron M Newman · 1985 to 2026
$19.1M
Stanford Training Program in Aging ResearchT32AG047126 · NIA · STANFORD UNIVERSITY · PI VYJEYANTHI S PERIYAKOIL, TONY WYSS-CORAY · 2014 to 2026
$4.3M
Role of NSD3 in regulation of cancer pathogenesisR01CA278940 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Or P. Gozani, Pawel K. Mazur · 2023 to 2026
$2.6M
Role of the METTL13 Lysine Methyltransferase in Signaling and CancerR01CA236118 · NCI · STANFORD UNIVERSITY · PI GOZANI, OR P., MAZUR, PAWEL K. · 2019 to 2023
$2.4M
Molecular Mechanisms of Mammalian SIRT6 FunctionR01AG050997 · NIA · PALO ALTO VETERANS INSTIT FOR RESEARCH · PI CHUA, KATRIN F · 2016 to 2020
$1.7M
NCI NIH HHS R01 CA236118NCI NIH HHS R01 CA278940NCI NIH HHS T32 CA009302NIA NIH HHS T32 AG047126NIH HHS R01AG050997NIH HHS R01CA236118
6 · The paper itself

Abstract

The tumor suppressor adenomatous polyposis coli (APC) is frequently mutated in colorectal cancers. APC and Axin are core components of a destruction complex that scaffolds GSK3β and CK1 to earmark β-catenin for proteosomal degradation. Disruption of APC results in pathologic stabilization of β-catenin and oncogenesis. However, the molecular mechanism by which APC promotes β-catenin degradation is unclear. Here, we find that the intrinsically disordered region (IDR) of APC, which contains multiple β-catenin and Axin interacting sites, undergoes liquid-liquid phase separation (LLPS) in vitro. Expression of the APC IDR in colorectal cells promotes Axin puncta formation and β-catenin degradation. Our results support the model that multivalent interactions between APC and Axin drives the β-catenin destruction complex to form biomolecular condensates in cells, which concentrate key components to achieve high efficient degradation of β-catenin.

Indexed as

Genes, APCAxin Proteinbeta CateninColorectal NeoplasmsHumansProteolysisAxin Proteinbeta CateninCTNNB1 protein, human

Identifiers

PMID33060621
PMCPMC7562749
OpenAlexW3093124326

What OpenQuestion holds

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LicenceCC BY
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.