Evidence map›Paper›PMID 26568304›Full record

ArticleOncogene2016

CHIP-mediated degradation of transglutaminase 2 negatively regulates tumor growth and angiogenesis in renal cancer.

B Min, H Park, S Lee, Y Li, J-M Choi, J Y Lee, J Kim, Y D Choi, Y-G Kwon, H-W Lee and 3 more

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
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  4. The Role of Transglutaminase 2 in Cancer: An Update.International journal of molecular sciences · 2024
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  8. Article
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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

13 authors at 4 institutions in 1 country.

B MinDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
H ParkDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
S LeeDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
Y LiDepartment of Bioengineering, College of Engineering, Hanyang University, Seoul, Republic of Korea.
J-M ChoiDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
J Y LeeDepartment of Urology, Yonsei University College of Medicine, Seoul, Republic of Korea.
J KimDepartment of Anatomy, School of Medicine, The Catholic University of Korea, Seoul, Republic of Korea.
Y D ChoiDepartment of Urology, Yonsei University College of Medicine, Seoul, Republic of Korea.
Y-G KwonDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
H-W LeeDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
S-C BaeDepartment of Biochemistry, College of Medicine, Chungbuk National University, Cheongju, Republic of Korea.
C-O YunDepartment of Bioengineering, College of Engineering, Hanyang University, Seoul, Republic of Korea.
K C ChungDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
Yonsei University · KRHanyang University · KRCatholic University of Korea · KRChungbuk National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The multifunctional enzyme transglutaminase 2 (TG2) primarily catalyzes cross-linking reactions of proteins via (γ-glutamyl) lysine bonds. Several recent findings indicate that altered regulation of intracellular TG2 levels affects renal cancer. Elevated TG2 expression is observed in renal cancer. However, the molecular mechanism underlying TG2 degradation is not completely understood. Carboxyl-terminus of Hsp70-interacting protein (CHIP) functions as an ubiquitin E3 ligase. Previous studies reveal that CHIP deficiency mice displayed a reduced life span with accelerated aging in kidney tissues. Here we show that CHIP promotes polyubiquitination of TG2 and its subsequent proteasomal degradation. In addition, TG2 upregulation contributes to enhanced kidney tumorigenesis. Furthermore, CHIP-mediated TG2 downregulation is critical for the suppression of kidney tumor growth and angiogenesis. Notably, our findings are further supported by decreased CHIP expression in human renal cancer tissues and renal cancer cells. The present work reveals that CHIP-mediated TG2 ubiquitination and proteasomal degradation represent a novel regulatory mechanism that controls intracellular TG2 levels. Alterations in this pathway result in TG2 hyperexpression and consequently contribute to renal cancer.

Indexed as

AnimalsCarcinoma, Renal CellCell Line, TumorGene Expression Regulation, NeoplasticGTP-Binding ProteinsHEK293 CellsHumansImmunoblottingImmunohistochemistryKidney NeoplasmsMaleMice, Inbred C57BLMice, NudeNeovascularization, PathologicProteasome Endopeptidase ComplexProtein BindingGTP-Binding ProteinsProteasome Endopeptidase ComplexProtein Glutamine gamma Glutamyltransferase 2STUB1 protein, humanTransglutaminasesUbiquitin-Protein Ligases

Identifiers

PMID26568304
OpenAlexW2202657505

What OpenQuestion holds

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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.