Evidence map›Paper›PMID 27409667›Full record

ArticleOncotarget2016

SUMOylation of PES1 upregulates its stability and function via inhibiting its ubiquitination.

Shujing Li, Miao Wang, Xinjian Qu, Zhaowei Xu, Yangyang Yang, Qiming Su, Huijian Wu

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-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

21 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  7. The SUMOylation and ubiquitination crosstalk in cancer.Journal of cancer research and clinical oncology · 2023
    Review
  8. Article
  9. Article
  10. Sumoylation regulates functional properties of the oocyte transcription factors SOHLH1 and NOBOX.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
    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

7 authors at 2 institutions in 1 country.

Shujing LiSchool of Life Science and Biotechnology, Dalian University of Technology, Dalian, China.
Miao WangSchool of Life Science and Biotechnology, Dalian University of Technology, Dalian, China.
Xinjian QuSchool of Life Science and Medicine, Dalian University of Technology, Panjin, China.
Zhaowei XuSchool of Life Science and Biotechnology, Dalian University of Technology, Dalian, China.
Yangyang YangSchool of Life Science and Biotechnology, Dalian University of Technology, Dalian, China.
Qiming SuSchool of Life Science and Medicine, Dalian University of Technology, Panjin, China.
Huijian WuSchool of Life Science and Biotechnology, Dalian University of Technology, Dalian, China.
Dalian University · CNDalian University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PES1 is a component of the PeBoW complex, which is required for the maturation of 28S and 5.8S ribosomal RNAs, as well as for the formation of the 60S ribosome. Deregulation of ribosomal biogenesis can contribute to carcinogenesis. In this study, we showed that PES1 could be modified by the small ubiquitin-like modifier (SUMO) SUMO-1, SUMO-2 and SUMO-3, and SUMOylation of PES1 was stimulated by estrogen (E2). One major SUMOylation site (K517) was identified in the C-terminal Glu-rich domain of PES1. Substitution of K517 with arginine abolished the SUMOylation of PES1. SUMOylation also stabilized PES1 through inhibiting its ubiquitination. In addition, PES1 SUMOylation positively regulated the estrogen signaling pathway. SUMOylation enhanced the ability of PES1 to promote estrogen receptor α (ERα)-mediated transcription by increasing the stability of ERα, both in the presence and absence of E2. Moreover, SUMOylation of PES1 also increased the proportion of S-phase cells in the cell cycle and promoted the proliferation of breast cancer cells both in vitro and in vivo. These findings showed that posttranslational modification of PES1 by SUMOylation may serve as a key factor that regulates the function of PES1 in vivo.

Indexed as

SumoylationUbiquitinationAnimalsBreast NeoplasmsCell CycleCell Line, TumorCell ProliferationChlorocebus aethiopsCOS CellsEstrogen Receptor alphaFemaleHumansMiceMice, Inbred BALB CMice, NudeNeoplasm TransplantationESR1 protein, humanEstrogen Receptor alphaPES1 protein, humanProteasome Endopeptidase ComplexProteinsRNA-Binding ProteinsRNA, Ribosomal, 28SRNA, Ribosomal, 5.8Sbreast cancerPES1SUMOylationubiquitination

Identifiers

PMID27409667
PMCPMC5226600
OpenAlexW2469206364

What OpenQuestion holds

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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.