Evidence map›Paper›PMID 17170702›Full record

ArticleThe EMBO journal2007

Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'.

Satoshi Yamasaki, Naoko Yagishita, Takeshi Sasaki, Minako Nakazawa, Yukihiro Kato, Tadayuki Yamadera, Eunkyung Bae, Sayumi Toriyama, Rie Ikeda, Lei Zhang and 22 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

103 citing papers in PubMed, 280 citations in OpenAlex.

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  19. Evaluation of a Novel Oncolytic Adenovirus SilencingInternational journal of molecular sciences · 2022
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43 more citing papers are in PubMed but not listed here.

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

32 authors at 10 institutions in 3 countries.

Satoshi YamasakiDepartment of Genome Science, Institute of Medical Science, St Marianna University School of Medicine, Kawasaki, Japan.
Naoko Yagishita
Takeshi Sasaki
Minako Nakazawa
Yukihiro Kato
Tadayuki Yamadera
Eunkyung Bae
Sayumi Toriyama
Rie Ikeda
Lei Zhang
Kazuko Fujitani
Eunkyung Yoo
Kaneyuki Tsuchimochi
Tomohiko Ohta
Natsumi Araya
Hidetoshi Fujita
Satoko Aratani
Katsumi Eguchi
Setsuro Komiya
Ikuro Maruyama
Nobuyo Higashi
Mitsuru Sato
Haruki Senoo
Takahiro Ochi
Shigeyuki Yokoyama
Tetsuya Amano
Jaeseob Kim
Steffen Gay
Akiyoshi Fukamizu
Kusuki Nishioka
Keiji Tanaka
Toshihiro Nakajima
St. Marianna University School of Medicine · JPAkita University · JPGenexine (South Korea) · KRKagoshima University · JPNagasaki University · JPNational Sagamihara Hospital · JPThe University of Tokyo · JPTokyo Metropolitan Institute of Medical Science · JPUniversity Hospital of Zurich · CHUniversity of Tsukuba · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synoviolin, also called HRD1, is an E3 ubiquitin ligase and is implicated in endoplasmic reticulum -associated degradation. In mammals, Synoviolin plays crucial roles in various physiological and pathological processes, including embryogenesis and the pathogenesis of arthropathy. However, little is known about the molecular mechanisms of Synoviolin in these actions. To clarify these issues, we analyzed the profile of protein expression in synoviolin-null cells. Here, we report that Synoviolin targets tumor suppressor gene p53 for ubiquitination. Synoviolin sequestrated and metabolized p53 in the cytoplasm and negatively regulated its cellular level and biological functions, including transcription, cell cycle regulation and apoptosis. Furthermore, these p53 regulatory functions of Synoviolin were irrelevant to other E3 ubiquitin ligases for p53, such as MDM2, Pirh2 and Cop1, which form autoregulatory feedback loops. Our results provide novel insights into p53 signaling mediated by Synoviolin.

Indexed as

AnimalsCell Line, TumorCytoplasmDrosophila melanogasterEndoplasmic ReticulumHumansPlasmidsProteasome Endopeptidase ComplexSignal TransductionTransfectionTumor Suppressor Protein p53UbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesProteasome Endopeptidase ComplexSYVN1 protein, humanTumor Suppressor Protein p53UbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID17170702
PMCPMC1782373
OpenAlexW1993964409

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.