Evidence map›Paper›PMID 29367604›Full record

ArticleCell death & disease2018

Covalent ISG15 conjugation to CHIP promotes its ubiquitin E3 ligase activity and inhibits lung cancer cell growth in response to type I interferon.

Lang Yoo, A-Rum Yoon, Chae-Ok Yun, Kwang Chul Chung

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

33 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. ISGylation: is our genome yearning for such a modification?Acta biochimica et biophysica Sinica · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. The Functional Roles of ISG15/ISGylation in Cancer.Molecules (Basel, Switzerland) · 2023
    Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. TRIM25: A central factor in breast cancer.World journal of clinical oncology · 2021
    Review
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

4 authors at 2 institutions in 1 country.

Lang YooDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, 03722, Korea.
A-Rum YoonDepartment of Bioengineering, College of Engineering, Hanyang University, Seoul, 04763, Korea.
Chae-Ok YunDepartment of Bioengineering, College of Engineering, Hanyang University, Seoul, 04763, Korea.
Kwang Chul ChungDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, 03722, Korea. kchung@yonsei.ac.kr.
Hanyang University · KRYonsei University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The carboxyl terminus of Hsp70-interacting protein (CHIP) acts as a ubiquitin E3 ligase and a link between the chaperones Hsp70/90 and the proteasome system, playing a vital role in maintaining protein homeostasis. CHIP regulates a number of proteins involved in a myriad of physiological and pathological processes, but the underlying mechanism of action via posttranslational modification has not been extensively explored. In this study, we investigated a novel modulatory mode of CHIP and its effect on CHIP enzymatic activity. ISG15, an ubiquitin-like modifier, is induced by type I interferon (IFN) stimulation and can be conjugated to target proteins (ISGylation). Here we demonstrated that CHIP may be a novel target of ISGylation in HEK293 cells stimulated with type I IFN. We also found that Lys143/144/145 and Lys287 residues in CHIP are important for and target residues of ISGylation. Moreover, ISGylation promotes the E3 ubiquitin ligase activity of CHIP, subsequently causing a decrease in levels of oncogenic c-Myc, one of its many ubiquitination targets, in A549 lung cancer cells and inhibiting A549 cell and tumor growth. In conclusion, the present study demonstrates that covalent ISG15 conjugation produces a novel CHIP regulatory mode that enhances the tumor-suppressive activity of CHIP, thereby contributing to the antitumor effect of type I IFN.

Indexed as

A549 CellsAnimalsCell ProliferationCytokinesHEK293 CellsHumansInterferon-alphaInterferon Type IIntracellular Signaling Peptides and ProteinsLung NeoplasmsLysineMaleMice, NudeNecrosisProteolysisProto-Oncogene Proteins c-mycCytokinesHERC5 protein, humanInterferon-alphaInterferon Type IIntracellular Signaling Peptides and ProteinsISG15 protein, humanLysineProto-Oncogene Proteins c-mycSTUB1 protein, humanTranscription FactorsTRIM25 protein, humanTripartite Motif ProteinsTumor Suppressor ProteinsUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID29367604
PMCPMC5833375
OpenAlexW2793377236

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.