Evidence map›Paper›PMID 35084653›Full record

ArticleMolecular neurobiology2022

COP1 Acts as a Ubiquitin Ligase for PCDH9 Ubiquitination and Degradation in Human Glioma.

Kunlin Zhou, Lei Wang, Zhiyuan Sun, Yuelin Liu, Yufu Zhu, Zhiyi Liu, Bin Zhang, Hengliang Shi

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Molecular neurobiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.5field-weighted citation impact, top 40% 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

6 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. The dual role of PCDH9 in tumors, neurological and developmental diseases.Medical oncology (Northwood, London, England) · 2025
    Review
  4. Article
  5. Article
  6. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Kunlin Zhou *Central Laboratory, The Affiliated Hospital of Xuzhou Medical University, Xuzhou, China.
Lei Wang *Central Laboratory, The Affiliated Hospital of Xuzhou Medical University, Xuzhou, China.
Zhiyuan SunCentral Laboratory, The Affiliated Hospital of Xuzhou Medical University, Xuzhou, China.
Yuelin LiuSchool of Clinical Medicine, Xuzhou Medical University, Xuzhou, Jiangsu, China.
Yufu ZhuInstitute of Nervous System Disease, Xuzhou Medical University, Xuzhou, China.
Zhiyi LiuInstitute of Digestive Diseases, Xuzhou Medical University, Xuzhou, China.
Bin ZhangInstitute of Digestive Diseases, Xuzhou Medical University, Xuzhou, China. Zhangbin209@163.com.
Hengliang ShiCentral Laboratory, The Affiliated Hospital of Xuzhou Medical University, Xuzhou, China. shl@xzhmu.edu.cn.ORCID http://orcid.org/0000-0002-9649-1910
Xuzhou Medical College · CN

Funding

the foundation of jiangsu provincial health department M2020082the foundation of xuzhou science and technology bureau KC20091the foundation of xuzhou science and technology bureau KC20128the foundation of xuzhou science and technology bureau KC20139the jiangsu provincial qing lan project and jiangsu provincial medical youth talent QNRC2016784the national innovation and entrepreneurship training program for college students 201910313019Zthe national innovation and entrepreneurship training program for college students 201910313026the national natural science foundation of china 81874081the natural science foundation of jiangsu province of china BK20181149the young science and technology innovation team of xuzhou medical university TD202006
6 · The paper itself

Abstract

Constitutive photomorphogenic 1 (COP1, also known as RFWD2), a ring-finger-type E3 ubiquitin ligase, has been reported to play a pivotal role in the regulation of cell growth, apoptosis, and DNA repair. Accumulating evidence has suggested that COP1 plays a role in tumorigenesis by triggering the ubiquitination and degradation of its substrates, but the potential mechanism remains unclear. In this study, COP1 was used as a bait in a yeast two-hybrid experiment to screen COP1-interacting proteins in a human brain cDNA library, and the results indicated that protocadherin 9 (PCDH9) was a potential binding protein of COP1. The interaction between and colocalization of COP1 and PCDH9 was further confirmed by coimmunoprecipitation (co-IP) assay and immunofluorescent staining. Subsequently, we demonstrated that COP1 acted as an E3 ligase to promote the ubiquitination and degradation of PCDH9 through the proteasome pathway in glioma cells. Furthermore, we identified that the type of COP1 mediated PCDH9 ubiquitination was Lys

Indexed as

GliomaUbiquitinCadherinsHumansProteasome Endopeptidase ComplexProtocadherinsUbiquitinationUbiquitin-Protein LigasesCadherinsCOP1 protein, humanPCDH9 protein, humanProteasome Endopeptidase ComplexProtocadherinsUbiquitinUbiquitin-Protein LigasesCOP1GliomaPCDH9Ubiquitination

Identifiers

PMID35084653
OpenAlexW4210458653

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.