Evidence map›Paper›PMID 29989488›Full record

ArticleAutophagy2018

The lysosomal membrane protein LAMP2A promotes autophagic flux and prevents SNCA-induced Parkinson disease-like symptoms in the Drosophila brain.

Abdul-Raouf Issa, Jun Sun, Céline Petitgas, Ana Mesquita, Amina Dulac, Marion Robin, Bertrand Mollereau, Andreas Jenny, Baya Chérif-Zahar, Serge Birman

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

75 citing papers in PubMed, 140 citations in OpenAlex.

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  15. Review
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  17. Parkinson's disease physiopathology-beyond theFrontiers in aging neuroscience · 2025
    Review
  18. Article
  19. Molecular mechanism on autophagy associated cardiovascular dysfunction inFrontiers in cell and developmental biology · 2025
    Review
  20. Article

15 more citing papers are in PubMed but not listed here.

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

10 authors at 3 institutions in 2 countries.

Abdul-Raouf Issaa Genes Circuits Rhythms and Neuropathology, Brain Plasticity Unit, CNRS, ESPCI Paris , PSL Research University , Paris , France.
Jun Suna Genes Circuits Rhythms and Neuropathology, Brain Plasticity Unit, CNRS, ESPCI Paris , PSL Research University , Paris , France.
Céline Petitgasa Genes Circuits Rhythms and Neuropathology, Brain Plasticity Unit, CNRS, ESPCI Paris , PSL Research University , Paris , France.
Ana Mesquitab Department of Developmental and Molecular Biology , Albert Einstein College of Medicine , New York , NY , USA.
Amina Dulaca Genes Circuits Rhythms and Neuropathology, Brain Plasticity Unit, CNRS, ESPCI Paris , PSL Research University , Paris , France.
Marion Robinc ENSL, UCBL, CNRS, LBMC, UMS 3444 Biosciences Lyon Gerland , Université de Lyon , Lyon , France.
Bertrand Mollereauc ENSL, UCBL, CNRS, LBMC, UMS 3444 Biosciences Lyon Gerland , Université de Lyon , Lyon , France.
Andreas Jennyb Department of Developmental and Molecular Biology , Albert Einstein College of Medicine , New York , NY , USA.
Baya Chérif-Zahara Genes Circuits Rhythms and Neuropathology, Brain Plasticity Unit, CNRS, ESPCI Paris , PSL Research University , Paris , France.
Serge Birmana Genes Circuits Rhythms and Neuropathology, Brain Plasticity Unit, CNRS, ESPCI Paris , PSL Research University , Paris , France.ORCID 0000-0002-4278-454X
Centre National de la Recherche Scientifique · FRAlbert Einstein College of Medicine · USUniversité Claude Bernard Lyon 1 · FR

Funding

ENDOSOMAL MICROAUTOPHAGY IN DROSOPHILAR01GM119160 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI JENNY, ANDREAS · 2017 to 2025
$3.9M
NIGMS NIH HHS R01 GM119160
6 · The paper itself

Abstract

The autophagy-lysosome pathway plays a fundamental role in the clearance of aggregated proteins and protection against cellular stress and neurodegenerative conditions. Alterations in autophagy processes, including macroautophagy and chaperone-mediated autophagy (CMA), have been described in Parkinson disease (PD). CMA is a selective autophagic process that depends on LAMP2A (lysosomal-associated membrane protein 2A), a mammal and bird-specific membrane glycoprotein that translocates cytosolic proteins containing a KFERQ-like peptide motif across the lysosomal membrane. Drosophila reportedly lack CMA and use endosomal microautophagy (eMI) as an alternative selective autophagic process. Here we report that neuronal expression of human LAMP2A protected Drosophila against starvation and oxidative stress, and delayed locomotor decline in aging flies without extending their lifespan. LAMP2A also prevented the progressive locomotor and oxidative defects induced by neuronal expression of PD-associated human SNCA (synuclein alpha) with alanine-to-proline mutation at position 30 (SNCA ABBREVIATIONS: Act5C: actin 5C; a.E.: after eclosion; Atg5: autophagy-related 5; Atg8a/LC3: autophagy-related 8a; CMA: chaperone-mediated autophagy; DHE: dihydroethidium; elav: embryonic lethal abnormal vision; eMI: endosomal microautophagy; ESCRT: endosomal sorting complexes required for transport; GABARAP: GABA typeA receptor-associated protein; Hsc70-4: heat shock protein cognate 4; HSPA8/Hsc70: heat shock protein family A (Hsp70) member 8; LAMP2: lysosomal associated membrane protein 2; MDA: malondialdehyde; PA-mCherry: photoactivable mCherry; PBS: phosphate-buffered saline; PCR: polymerase chain reaction; PD: Parkinson disease; Ref(2)P/p62: refractory to sigma P; ROS: reactive oxygen species; RpL32/rp49: ribosomal protein L32; RT-PCR: reverse transcription polymerase chain reaction; SING: startle-induced negative geotaxis; SNCA/α-synuclein: synuclein alpha; SQSTM1/p62: sequestosome 1; TBS: Tris-buffered saline; UAS: upstream activating sequence.

Indexed as

Drosophilaalpha-SynucleinAnimalsAnimals, Genetically ModifiedAutophagyBrainDisease Models, AnimalHumansLocomotionLysosomal-Associated Membrane Protein 2NeuroprotectionOxidative StressParkinson DiseasePhenotypeSignal Transductionalpha-SynucleinLAMP2 protein, humanLysosomal-Associated Membrane Protein 2Autophagy-lysosome pathwayDrosophila melanogasterlysosomal-associated membrane protein 2A (LAMP2A)neuroprotectionParkinson diseasesynuclein alpha (SNCA)

Identifiers

PMID29989488
PMCPMC6152503
OpenAlexW2882031129

What OpenQuestion holds

Textmetadata
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.