Evidence map›Paper›PMID 34347505›Full record

ArticleMolecular biology of the cell2021

Mff oligomerization is required for Drp1 activation and synergy with actin filaments during mitochondrial division.

Ao Liu, Frieda Kage, Henry N Higgs

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
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  7. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
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  12. Review
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  18. Review
  19. The multiple links between actin and mitochondria.Nature reviews. Molecular cell biology · 2023
    Review
  20. Article
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

3 authors at 1 institution in 1 country.

Ao LiuDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH 03755.
Frieda KageDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH 03755.
Henry N HiggsDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH 03755.
Dartmouth College · US

Funding

Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MADDEN, DEAN R · 2016 to 2025
$25.9M
The impact of dynamic actin polymerization on mitochondrial dynamics and functionR35GM122545 · NIGMS · DARTMOUTH COLLEGE · PI HENRY N HIGGS · 2017 to 2026
$7.7M
INF2 in kidney function and dysfunctionR01DK088826 · NIDDK · BETH ISRAEL DEACONESS MEDICAL CENTER · PI HENRY N HIGGS, MARTIN R. POLLAK · 2010 to 2026
$6.3M
NIDDK NIH HHS R01 DK088826NIGMS NIH HHS P20 GM113132NIGMS NIH HHS R35 GM122545
6 · The paper itself

Abstract

Mitochondrial division is an important cellular process in both normal and pathological conditions. The dynamin GTPase Drp1 is a central mitochondrial division protein, driving constriction of the outer mitochondrial membrane (OMM). In mammals, the OMM protein mitochondrial fission factor (Mff) is a key receptor for recruiting Drp1 from the cytosol to the mitochondrion. Actin filaments are also important in Drp1 recruitment and activation. The manner in which Mff and actin work together in Drp1 activation is unknown. Here we show that Mff is an oligomer (most likely a trimer) that dynamically associates and disassociates through its C-terminal coiled coil, with a

Indexed as

Actin CytoskeletonActinsCytosolDynaminsGTP PhosphohydrolasesHumansMembrane ProteinsMicrotubule-Associated ProteinsMitochondriaMitochondrial DynamicsMitochondrial MembranesMitochondrial ProteinsPeptide Elongation FactorsProtein BindingProtein MultimerizationActinsDNM1L protein, humanDynaminsGTP PhosphohydrolasesMembrane ProteinsMff protein, humanMicrotubule-Associated ProteinsMitochondrial ProteinsPeptide Elongation Factors

Identifiers

PMID34347505
PMCPMC8684745
OpenAlexW3191178710

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.