Evidence map›Paper›PMID 30516433›Full record

ArticleMolecular biology of the cell2019

Cyclin C directly stimulates Drp1 GTP affinity to mediate stress-induced mitochondrial hyperfission.

Vidyaramanan Ganesan, Stephen D Willis, Kai-Ti Chang, Samuel Beluch, Katrina F Cooper, Randy Strich

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 38 citations in OpenAlex.

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  19. Molecular Basis of Mitochondrial and Peroxisomal Division Machineries.International journal of molecular sciences · 2020
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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

6 authors at 2 institutions in 1 country.

Vidyaramanan GanesanDepartment of Molecular Biology, Graduate School of Biomedical Sciences, Rowan University School of Osteopathic Medicine, Stratford, NJ 08084.
Stephen D WillisDepartment of Molecular Biology, Graduate School of Biomedical Sciences, Rowan University School of Osteopathic Medicine, Stratford, NJ 08084.
Kai-Ti ChangDepartment of Molecular Biology, Graduate School of Biomedical Sciences, Rowan University School of Osteopathic Medicine, Stratford, NJ 08084.
Samuel BeluchDepartment of Molecular Biology, Graduate School of Biomedical Sciences, Rowan University School of Osteopathic Medicine, Stratford, NJ 08084.
Katrina F CooperDepartment of Molecular Biology, Graduate School of Biomedical Sciences, Rowan University School of Osteopathic Medicine, Stratford, NJ 08084.
Randy StrichDepartment of Molecular Biology, Graduate School of Biomedical Sciences, Rowan University School of Osteopathic Medicine, Stratford, NJ 08084.
Rowan University · USRutgers, The State University of New Jersey · US

Funding

Stress regulated mitochondrial dynamicsR01GM113052 · NIGMS · ROWAN UNIVERSITY SCHOOL/OSTEOPATHIC MED · PI STRICH, RANDY S · 2014 to 2017
$1.3M
Stress induced signaling and cyclin C regulation in yeastR15GM113196 · NIGMS · ROWAN UNIVERSITY SCHOOL/OSTEOPATHIC MED · PI COOPER, KATRINA FRANCES · 2015 to 2015
$396k
NIGMS NIH HHS R01 GM113052NIGMS NIH HHS R15 GM113196
6 · The paper itself

Abstract

Mitochondria exist in an equilibrium between fragmented and fused states that shifts heavily toward fission in response to cellular damage. Nuclear-to-cytoplasmic cyclin C relocalization is essential for dynamin-related protein 1 (Drp1)-dependent mitochondrial fission in response to oxidative stress. This study finds that cyclin C directly interacts with the Drp1 GTPase domain, increases its affinity to GTP, and stimulates GTPase activity in vitro. In addition, the cyclin C domain that binds Drp1 is contained within the non-Cdk binding second cyclin box domain common to all cyclin family members. This interaction is important, as this domain is sufficient to induce mitochondrial fission when expressed in mouse embryonic fibroblasts in the absence of additional stress signals. Using gel filtration chromatography and negative stain electron microscopy, we found that cyclin C interaction changes the geometry of Drp1 oligomers in vitro. High-molecular weight low-GTPase activity oligomers in the form of short filaments and rings were diminished, while dimers and elongated filaments were observed. Our results support a model in which cyclin C binding stimulates the reduction of low-GTPase activity Drp1 oligomers into dimers capable of producing high-GTPase activity filaments.

Indexed as

Stress, PhysiologicalActin CytoskeletonAnimalsCyclin CFibroblastsGuanosine TriphosphateHumansMiceMicrotubule-Associated ProteinsMitochondriaProtein BindingProtein DomainsProtein MultimerizationCyclin CGuanosine TriphosphateMicrotubule-Associated Proteins

Identifiers

PMID30516433
PMCPMC6589575
OpenAlexW2903091755

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.