Evidence map›Paper›PMID 31555141›Full record

ArticleFrontiers in physiology2019

A Unique SUMO-Interacting Motif of Trx2 Is Critical for Its Mitochondrial Presequence Processing and Anti-oxidant Activity.

Chaofei Chen, Kang Wang, Haifeng Zhang, Huanjiao Jenny Zhou, Yuxin Chen, Wang Min

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in physiology, 2019. 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
0.7field-weighted citation impact, top 31% 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, 17 citations in OpenAlex.

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  8. Journal of Zhejiang University. Science. B · 2023
    Article
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  14. SUMOylation-Mediated Response to Mitochondrial Stress.International journal of molecular sciences · 2020
    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

6 authors at 3 institutions in 2 countries.

Chaofei ChenCenter for Translational Medicine, The First Affiliated Hospital, Sun Yat-sen University, Guangzhou, China.
Kang WangCenter for Translational Medicine, The First Affiliated Hospital, Sun Yat-sen University, Guangzhou, China.
Haifeng ZhangDepartment of Pathology, Vascular Biology and Therapeutics Program, Yale School of Medicine, Yale University, New Haven, CT, United States.
Huanjiao Jenny ZhouDepartment of Pathology, Vascular Biology and Therapeutics Program, Yale School of Medicine, Yale University, New Haven, CT, United States.
Yuxin ChenDepartment of Laboratory Medicine, Nanjing Drum Tower Hospital, Nanjing University Medical School, Nanjing, China.
Wang MinDepartment of Pathology, Vascular Biology and Therapeutics Program, Yale School of Medicine, Yale University, New Haven, CT, United States.
Yale University · USNanjing Drum Tower Hospital · CNSun Yat-sen University · CN

Funding

The role of signaling molecule AIP1 in pathological angiogenesisR01HL115148 · NHLBI · YALE UNIVERSITY · PI KYRIAKIDES, THEMIS R · 2013 to 2021
$3.6M
STRESS SIGNALING PATHWAYS LINKING ENDOTHELIAL INJURY TO GRAFT ARTERIOSCLEROSISR01HL109420 · NHLBI · YALE UNIVERSITY · PI POBER, JORDAN S · 2012 to 2020
$3.3M
NHLBI NIH HHS R01 HL109420NHLBI NIH HHS R01 HL115148
6 · The paper itself

Abstract

objectiveMitochondrial thioredoxin 2 (Trx2) is a vital mitochondrial redox protein that mediates normal protein thiol reduction and provides electrons to peroxiredoxin 3 (Prx3) to scavenge H APPROACH AND

resultsHere we show that excess ROS induce endothelial cell senescence concomitant with an attenuation of Trx2 processing in which Trx2 presequence [i.e., mitochondrial targeting signal peptide (MTS)] is cleaved to generate a mature form. Mutation analyses indicate that Trx2 processing is mediated by mitochondrial processing peptidase (MPP) and mitochondrial intermediate peptidase (MIP)-recognition sites within the MTS. Interestingly, a mutation at a SUMO- interacting motif (SIM), but not the catalytic sites within the mature Trx2 protein, completely blocks Trx2 processing with no effect on Trx2 mitochondrial targeting. Consistently, chemical inhibition of protein SUMOylation attenuates, while SUMOylation agonist promotes, Trx2 processing. Moreover, we identify the α-MPP subunit is a SUMOylated protein that potentially mediates Trx2-binding and cleavage. Furthermore, the unprocessed form of Trx2-SIM is unable to protect cells from both ROS generation and oxidative stress-induced cellular senescence.

conclusionOur study reveals that a unique SUMO-interacting motif of Trx2 is critical for its mitochondrial processing and subsequent anti-oxidant/antisenescence activities.

Indexed as

mitochondriasenescenceSUMO-interacting motifsumoylationthioredoxin-2

Identifiers

PMID31555141
PMCPMC6727865
OpenAlexW2966156588

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.