Evidence map›Paper›PMID 35932293›Full record

ArticleCellular and molecular life sciences : CMLS2022

Neuronal-specific septin-3 binds Atg8/LC3B, accumulates and localizes to autophagosomes during induced autophagy.

Vilmos Tóth, Henrietta Vadászi, Lilla Ravasz, Dániel Mittli, Dominik Mátyás, Tamás Molnár, András Micsonai, Tamás Szaniszló, Péter Lőrincz, Réka Á Kovács and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.6field-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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. SEPT3 as a Potential Molecular Target of Triple-Negative Breast Cancer.International journal of general medicine · 2024
    Article
  7. The Small-Molecule Enhancers of Autophagy AUTEN-67 and -99 Delay Ageing inInternational journal of molecular sciences · 2023
    Article
  8. Article
  9. Review
  10. Article
  11. 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

16 authors at 2 institutions in 2 countries.

Vilmos TóthELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
Henrietta VadásziELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
Lilla RavaszELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
Dániel MittliELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
Dominik MátyásELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
Tamás MolnárDepartment of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
András MicsonaiELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
Tamás SzaniszlóDepartment of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
Péter LőrinczDepartment of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest, Hungary.
Réka Á KovácsELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
Tünde JuhászInstitute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.
Tamás Beke-SomfaiInstitute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.
Gábor JuhászELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
Balázs András GyörffyELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
Katalin A KékesiELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary.
József KardosELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary. kardos@elte.hu.ORCID http://orcid.org/0000-0002-2135-2932
Eötvös Loránd University · HUInstitute of Materials and Environmental Chemistry · HU

Funding

Hungarian Academy of Sciences BO-00514-21-8Nemzeti Kutatási, Fejlesztési és Innovaciós Alap 2017-1.2.1-NKP-2017-00002Nemzeti Kutatási, Fejlesztési és Innovaciós Alap FIEK_16-1-2016-0005Nemzeti Kutatási, Fejlesztési és Innovaciós Alap FK 138851Nemzeti Kutatási, Fejlesztési és Innovaciós Alap K138937Nemzeti Kutatási, Fejlesztési és Innovaciós Alap PD135510Nemzeti Kutatási, Fejlesztési és Innovaciós Alap ÚNKP-21-5-ELTE-1122
6 · The paper itself

Abstract

In synapses that show signs of local apoptosis and mitochondrial stress and undergo neuro-immunological synapse pruning, an increase in the levels of the presynaptic protein, neuronal-specific septin-3 can be observed. Septin-3 is a member of the septin GTPase family with the ability to form multimers and contribute to the cytoskeleton. However, the function of septin-3 remains elusive. Here, we provide evidence that septin-3 is capable of binding the most-studied autophagy protein Atg8 homolog microtubule-associated protein 1 light chain 3B (LC3B), besides another homolog, GABA receptor-associated protein-like 2 (GABARAPL2). Moreover, we demonstrate that colocalization of septin-3 and LC3B increases upon chemical autophagy induction in primary neuronal cells. Septin-3 is accumulated in primary neurons upon autophagy enhancement or blockade, similar to autophagy proteins. Using electron microscopy, we also show that septin-3 localizes to LC3B positive membranes and can be found at mitochondria. However, colocalization results of septin-3 and the early mitophagy marker PTEN-induced kinase 1 (PINK1) do not support that binding of septin-3 to mitochondria is mitophagy related. We conclude that septin-3 correlates with synaptic/neuronal autophagy, binds Atg8 and localizes to autophagic membranes that can be enhanced with chemical autophagy induction. Based on our results, elevated septin-3 levels might indicate enhanced or impeded autophagy in neurons.

Indexed as

AutophagosomesSeptinsAutophagyMicrotubule-Associated ProteinsMitophagyNeuronsMicrotubule-Associated ProteinsSeptinsAtg8AutophagyLIRNeuronal autophagySeptinSynaptic autophagySynaptic pruning

Identifiers

PMID35932293
PMCPMC9356936
OpenAlexW4290034393

What OpenQuestion holds

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LicenceCC BY
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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.