Evidence map›Paper›PMID 28245560›Full record

ReviewInternational journal of molecular sciences2017

The Regulations of Deubiquitinase USP15 and Its Pathophysiological Mechanisms in Diseases.

Chon-Kit Chou, Yu-Ting Chang, Michal Korinek, Yei-Tsung Chen, Ya-Ting Yang, Steve Leu, I-Ling Lin, Chin-Ju Tang, Chien-Chih Chiu

Erratum issuedOpen access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2017. 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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

35 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Ubiquitin proteasome system in cardiac fibrosis.Journal of advanced research · 2025
    Review
  4. Unravelling Heterozygosity-Rich Regions in the Holstein Genome.Animals : an open access journal from MDPI · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Observational
  18. Review
  19. Review
  20. The Multifaceted Roles of USP15 in Signal Transduction.International journal of molecular sciences · 2021
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Chon-Kit ChouGraduate Institute of Natural Products, Kaohsiung Medical University, Kaohsiung 807, Taiwan. fatchou1988@hotmail.com.
Yu-Ting ChangDepartment of Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan. c.jasmine8306@gmail.com.
Michal KorinekGraduate Institute of Natural Products, Kaohsiung Medical University, Kaohsiung 807, Taiwan. mickorinek@hotmail.com.
Yei-Tsung ChenDepartment of Medicine, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117, Singapore. mdccyt@nus.edu.sg.
Ya-Ting YangDepartment of Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan. tinayang101@gmail.com.
Steve LeuDepartment of Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan. st.leu.tw@gmail.com.
I-Ling LinDepartment of Medical Laboratory Science and Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan. linili@cc.kmu.edu.tw.
Chin-Ju TangDepartment of Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan. candace0602@gmail.com.
Chien-Chih ChiuDepartment of Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan. cchiu@kmu.edu.tw.
Kaohsiung Medical University · TWNational Sun Yat-sen University · TWNational University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deubiquitinases (DUBs) play a critical role in ubiquitin-directed signaling by catalytically removing the ubiquitin from substrate proteins. Ubiquitin-specific protease 15 (USP15), a member of the largest subfamily of cysteine protease DUBs, contains two conservative cysteine (Cys) and histidine (His) boxes. USP15 harbors two zinc-binding motifs that are essential for recognition of poly-ubiquitin chains. USP15 is grouped into the same category with USP4 and USP11 due to high degree of homology in an N-terminal region consisting of domains present in ubiquitin-specific proteases (DUSP) domain and ubiquitin-like (UBL) domain. USP15 cooperates with COP9 signalosome complex (CSN) to maintain the stability of cullin-ring ligase (CRL) adaptor proteins by removing the conjugated ubiquitin chains from RBX1 subunit of CRL. USP15 is also implicated in the stabilization of the human papillomavirus type 16 E6 oncoprotein, adenomatous polyposis coli, and IκBα. Recently, reports have suggested that USP15 acts as a key regulator of TGF-β receptor-signaling pathways by deubiquitinating the TGF-β receptor itself and its downstream transducers receptor-regulated SMADs (R-SMADs), including SMAD1, SMAD2, and SMAD3, thus activating the TGF-β target genes. Although the importance of USP15 in pathologic processes remains ambiguous so far, in this review, we endeavor to summarize the literature regarding the relationship of the deubiquitinating action of USP15 with the proteins involved in the regulation of Parkinson's disease, virus infection, and cancer-related signaling networks.

Indexed as

Disease SusceptibilityUbiquitinationAnimalsCell Transformation, NeoplasticChromosome MappingDrug Resistance, NeoplasmGene ExpressionGene Expression RegulationHumansIntracellular SpaceIsoenzymesProtein BindingProtein Interaction Domains and MotifsProtein TransportSignal TransductionStructure-Activity RelationshipIsoenzymesUbiquitin-Specific ProteasesUSP15 protein, humancancer-related signaling networksdeubiquitinaseIκBαParkinson’s diseaseTGF-βubiquitin-specific protease 15

Identifiers

PMID28245560
PMCPMC5372499
OpenAlexW2590487999

What OpenQuestion holds

Textmetadata
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.