Evidence map›Paper›PMID 38279052›Full record

ArticleCellular and molecular life sciences : CMLS2024

APC mutations disrupt β-catenin destruction complex condensates organized by Axin phase separation.

Dan Zhang, Qi-Qi Ni, Shu-Yang Wang, Wen-Feng He, Ze-Xuan Hong, Hui-Ye Liu, Xiao-Hong Chen, Li-Jie Chen, Fang-Yi Han, Ling-Jie Zhang and 4 more

Open access · goldAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2024. 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
6.3field-weighted citation impact, top 3% 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, 27 citations in OpenAlex.

  1. Article
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  3. Molecules (Basel, Switzerland) · 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

14 authors at 3 institutions in 1 country.

Dan Zhang *Department of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China.
Qi-Qi Ni *Department of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China.
Shu-Yang WangDepartment of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China.
Wen-Feng HeDepartment of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China.
Ze-Xuan HongDepartment of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China.
Hui-Ye LiuDepartment of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China.
Xiao-Hong ChenDepartment of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China.
Li-Jie ChenDepartment of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China.
Fang-Yi HanDepartment of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China.
Ling-Jie ZhangDepartment of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China.
Xiao-Ming LiDepartment of Pathology, The People's Hospital of Baoan Shenzhen, Shenzhen, Guangdong, China. lixm@lzu.edu.cn.
Yan-Qing DingDepartment of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China. dyqsmu@126.com.
Hong-Li JiaoDepartment of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China. 25048195@qq.com.
Ya-Ping YeDepartment of Pathology, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong, China. yeyp1980@126.com.ORCID http://orcid.org/0000-0001-5376-0124
Key Laboratory of Guangdong Province · CNRunze (China) · CNShenzhen Bao'an District People's Hospital · CN

Funding

National Natural Science Foundation of China 81972754National Natural Science Foundation of China 81972756National Natural Science Foundation of China 82072713National Natural Science Foundation of China 82173185National Natural Science Foundation of China 82273218Natural Science Foundation of Guangdong Province 2022A1515010544Postdoctoral Research Foundation of China 2022M711506
6 · The paper itself

Abstract

The Wnt/β-catenin pathway is critical to maintaining cell fate decisions. Recent study showed that liquid-liquid-phase separation (LLPS) of Axin organized the β-catenin destruction complex condensates in a normal cellular state. Mutations inactivating the APC gene are found in approximately 80% of all human colorectal cancer (CRC). However, the molecular mechanism of the formation of β-catenin destruction complex condensates organized by Axin phase separation and how APC mutations impact the condensates are still unclear. Here, we report that the β-catenin destruction complex, which is constructed by Axin, was assembled condensates via a phase separation process in CRC cells. The key role of wild-type APC is to stabilize destruction complex condensates. Surprisingly, truncated APC did not affect the formation of condensates, and GSK 3β and CK1α were unsuccessfully recruited, preventing β-catenin phosphorylation and resulting in accumulation in the cytoplasm of CRCs. Besides, we propose that the phase separation ability of Axin participates in the nucleus translocation of β-catenin and be incorporated and concentrated into transcriptional condensates, affecting the transcriptional activity of Wnt signaling pathway.

Indexed as

Axin Signaling Complexbeta CateninAdenomatous Polyposis Coli ProteinAxin ProteinHumansMutationPhase SeparationWnt Signaling PathwayAdenomatous Polyposis Coli ProteinAxin ProteinAxin Signaling Complexbeta CateninAPC mutationsAxinColorectal cancerDestruction complexNuclear transportPhase separationWnt/β-catenin signaling pathway

Identifiers

PMID38279052
PMCPMC10817841
OpenAlexW4391282713

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.