Evidence map›Paper›PMID 28262828›Full record

ArticleScientific reports2017

SENP3-mediated deSUMOylation of Drp1 facilitates interaction with Mff to promote cell death.

Chun Guo, Kevin A Wilkinson, Ashley J Evans, Philip P Rubin, Jeremy M Henley

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

54 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
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  9. DRP1, fission and apoptosis.Cell death discovery · 2025
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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

5 authors at 1 institution in 1 country.

Chun GuoSchool of Biochemistry, Centre for Synaptic Plasticity, Biomedical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Kevin A WilkinsonSchool of Biochemistry, Centre for Synaptic Plasticity, Biomedical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Ashley J EvansSchool of Biochemistry, Centre for Synaptic Plasticity, Biomedical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Philip P RubinSchool of Biochemistry, Centre for Synaptic Plasticity, Biomedical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Jeremy M HenleySchool of Biochemistry, Centre for Synaptic Plasticity, Biomedical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
University of Bristol · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F00723X/1Biotechnology and Biological Sciences Research Council BB/K014358/1British Heart Foundation PG/14/60/31014Medical Research CouncilParkinson's UK G-1605Wellcome Trust
6 · The paper itself

Abstract

The GTPase dynamin-related protein 1 (Drp1) is essential for physiological and pathophysiological mitochondrial fission. DeSUMOylation of Drp1 by the enzyme SENP3 promotes cell death during reperfusion after ischaemia by enhancing Drp1 partitioning to the mitochondrial outer membrane (MOM), which causes cytochrome c release and apoptosis. However, how deSUMOylation recruits Drp1 to the MOM is unknown. Here we show that deSUMOylation selectively promotes Drp1 binding to the MOM resident adaptor protein mitochondrial fission factor (Mff). Consistent with this, preventing Drp1 SUMOylation by mutating the SUMO acceptor sites enhances binding to Mff. Conversely, increasing Drp1 SUMOylation by knocking down SENP3 reduces both Drp1 binding to Mff and stress-induced cytochrome c release. Directly tethering Drp1 to the MOM bypasses the need for Mff to evoke cytochrome c release, and occludes the effect of SENP3 overexpression. Thus, Drp1 deSUMOylation promotes cell death by enhancing Mff-mediated mitochondrial recruitment. These data provide a mechanistic explanation for how the SUMOylation status of Drp1 acts as a key switch in cell death/survival decisions following extreme cell stress.

Indexed as

ApoptosisCysteine EndopeptidasesCytochromes cDynaminsGTP PhosphohydrolasesHEK293 CellsHeLa CellsHumansMembrane ProteinsMicrotubule-Associated ProteinsMitochondriaMitochondrial ProteinsProtein BindingRNA InterferenceSumoylationCysteine EndopeptidasesCytochromes cDNM1L protein, humanDynaminsGTP PhosphohydrolasesMembrane ProteinsMff protein, humanMicrotubule-Associated ProteinsMitochondrial ProteinsSENP3 protein, human

Identifiers

PMID28262828
PMCPMC5338345
OpenAlexW2592600610

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.