Evidence map›Paper›PMID 32708307›Full record

ArticleBiomolecules2020

The GDP-Bound State of Mitochondrial Mfn1 Induces Membrane Adhesion of Apposing Lipid Vesicles through a Cooperative Binding Mechanism.

Andrés Tolosa-Díaz, Víctor G Almendro-Vedia, Paolo Natale, Iván López-Montero

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 46% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Mfn2-dependent fusion pathway of PE-enriched micron-sized vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. A detailed review of pharmacology of MFN1 (mitofusion-1)-mediated mitochondrial dynamics: Implications for cellular health and diseases.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024
    Review
  3. Article
  4. Mitofusins: from mitochondria to fertility.Cellular and molecular life sciences : CMLS · 2022
    Review
  5. 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

4 authors at 1 institution in 1 country.

Andrés Tolosa-DíazDto. Química Física, Universidad Complutense de Madrid, Avenida Complutense s/n, 28040 Madrid, Spain.
Víctor G Almendro-VediaDto. Química Física, Universidad Complutense de Madrid, Avenida Complutense s/n, 28040 Madrid, Spain.ORCID 0000-0002-7297-1901
Paolo NataleDto. Química Física, Universidad Complutense de Madrid, Avenida Complutense s/n, 28040 Madrid, Spain.ORCID 0000-0002-4759-0816
Iván López-MonteroDto. Química Física, Universidad Complutense de Madrid, Avenida Complutense s/n, 28040 Madrid, Spain.ORCID 0000-0001-8131-6063
Universidad Complutense de Madrid · ES

Funding

FP7 Ideas: European Research Council 338133
6 · The paper itself

Abstract

Mitochondria are double-membrane organelles that continuously undergo fission and fusion. Outer mitochondrial membrane fusion is mediated by the membrane proteins mitofusin 1 (Mfn1) and mitofusin 2 (Mfn2), carrying a GTP hydrolyzing domain (GTPase) and two coiled-coil repeats. The detailed mechanism on how the GTP hydrolysis allows Mfns to approach adjacent membranes into proximity and promote their fusion is currently under debate. Using model membranes built up as giant unilamellar vesicles (GUVs), we show here that Mfn1 promotes membrane adhesion of apposing lipid vesicles. The adhesion forces were sustained by the GDP-bound state of Mfn1 after GTP hydrolysis. In contrast, the incubation with the GDP:AlF 4 - , which mimics the GTP transition state, did not induce membrane adhesion. Due to the flexible nature of lipid membranes, the adhesion strength depended on the surface concentration of Mfn1 through a cooperative binding mechanism. We discuss a possible scenario for the outer mitochondrial membrane fusion based on the modulated action of Mfn1.

Indexed as

Membrane FusionGTP PhosphohydrolasesGuanosine DiphosphateHumansHydrolysisMitochondriaMitochondrial Membrane Transport ProteinsProtein BindingUnilamellar LiposomesGTP PhosphohydrolasesGuanosine DiphosphateMfn1 protein, humanMitochondrial Membrane Transport ProteinsUnilamellar Liposomesgiant vesiclesGTPasemembrane fusionmitochondriamitofusin 1

Identifiers

PMID32708307
PMCPMC7407159
OpenAlexW3044592344

What OpenQuestion holds

Textmetadata
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.