Evidence map›Paper›PMID 31852899›Full record

ArticleNature communications2019

SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection.

Nils C Gassen, Daniela Niemeyer, Doreen Muth, Victor M Corman, Silvia Martinelli, Alwine Gassen, Kathrin Hafner, Jan Papies, Kirstin Mösbauer, Andreas Zellner and 9 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 250 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
250citing papers in PubMed, 1 pooled it
41.7field-weighted citation impact, top 1% 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

250 citing papers in PubMed, 1 synthesis or guideline pooled it, 369 citations in OpenAlex.

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  16. E3 ubiquitin ligase SKP2 limits autophagosome formation duringFrontiers in cellular and infection microbiology · 2026
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190 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

19 authors at 8 institutions in 4 countries.

Nils C GassenDepartment of Translational Research in Psychiatry, Max Planck Institute of Psychiatry, Kraepelinstr. 10, 80804, Munich, Germany. ncgassen@psych.mpg.de.
Daniela NiemeyerInstitute of Virology, Charité-Universitätsmedizin Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Charitéplatz 1, 10117, Berlin, Germany.ORCID http://orcid.org/0000-0002-1897-6365
Doreen MuthInstitute of Virology, Charité-Universitätsmedizin Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Charitéplatz 1, 10117, Berlin, Germany.
Victor M CormanInstitute of Virology, Charité-Universitätsmedizin Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Charitéplatz 1, 10117, Berlin, Germany.ORCID http://orcid.org/0000-0002-3605-0136
Silvia MartinelliDepartment of Translational Research in Psychiatry, Max Planck Institute of Psychiatry, Kraepelinstr. 10, 80804, Munich, Germany.
Alwine GassenFaculty of Biology, Genetics, Ludwig-Maximilian-University Munich (LMU), 82152, Martinsried, Germany.
Kathrin HafnerDepartment of Translational Research in Psychiatry, Max Planck Institute of Psychiatry, Kraepelinstr. 10, 80804, Munich, Germany.
Jan PapiesInstitute of Virology, Charité-Universitätsmedizin Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Charitéplatz 1, 10117, Berlin, Germany.
Kirstin MösbauerInstitute of Virology, Charité-Universitätsmedizin Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Charitéplatz 1, 10117, Berlin, Germany.
Andreas ZellnerDepartment of Translational Research in Psychiatry, Max Planck Institute of Psychiatry, Kraepelinstr. 10, 80804, Munich, Germany.
Anthony S ZannasDepartment of Translational Research in Psychiatry, Max Planck Institute of Psychiatry, Kraepelinstr. 10, 80804, Munich, Germany.ORCID http://orcid.org/0000-0002-6897-9652
Alexander HerrmannHIV-Cell-Interactions Group, Institute of Virology, German Research Center for Environmental Health, Ingolstädter Landstr. 1, 85764, Neuherberg, Germany.ORCID http://orcid.org/0000-0002-2749-9003
Florian HolsboerDepartment of Translational Research in Psychiatry, Max Planck Institute of Psychiatry, Kraepelinstr. 10, 80804, Munich, Germany.
Ruth Brack-WernerHIV-Cell-Interactions Group, Institute of Virology, German Research Center for Environmental Health, Ingolstädter Landstr. 1, 85764, Neuherberg, Germany.
Michael BoshartFaculty of Biology, Genetics, Ludwig-Maximilian-University Munich (LMU), 82152, Martinsried, Germany.
Bertram Müller-MyhsokDepartment of Translational Research in Psychiatry, Max Planck Institute of Psychiatry, Kraepelinstr. 10, 80804, Munich, Germany.
Christian DrostenInstitute of Virology, Charité-Universitätsmedizin Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Charitéplatz 1, 10117, Berlin, Germany.
Marcel A MüllerInstitute of Virology, Charité-Universitätsmedizin Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Charitéplatz 1, 10117, Berlin, Germany.ORCID http://orcid.org/0000-0003-2242-5117
Theo ReinDepartment of Translational Research in Psychiatry, Max Planck Institute of Psychiatry, Kraepelinstr. 10, 80804, Munich, Germany. theorein@psych.mpg.de.ORCID http://orcid.org/0000-0003-2850-4289
Humboldt-Universität zu Berlin · DEMax Planck Institute of Psychiatry · DEHelmholtz Zentrum München · DELudwig-Maximilians-Universität München · DESechenov University · RUUniversity of Bonn · DEUniversity of Liverpool · GBUniversity of North Carolina at Chapel Hill · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is an essential cellular process affecting virus infections and other diseases and Beclin1 (BECN1) is one of its key regulators. Here, we identified S-phase kinase-associated protein 2 (SKP2) as E3 ligase that executes lysine-48-linked poly-ubiquitination of BECN1, thus promoting its proteasomal degradation. SKP2 activity is regulated by phosphorylation in a hetero-complex involving FKBP51, PHLPP, AKT1, and BECN1. Genetic or pharmacological inhibition of SKP2 decreases BECN1 ubiquitination, decreases BECN1 degradation and enhances autophagic flux. Middle East respiratory syndrome coronavirus (MERS-CoV) multiplication results in reduced BECN1 levels and blocks the fusion of autophagosomes and lysosomes. Inhibitors of SKP2 not only enhance autophagy but also reduce the replication of MERS-CoV up to 28,000-fold. The SKP2-BECN1 link constitutes a promising target for host-directed antiviral drugs and possibly other autophagy-sensitive conditions.

Indexed as

AnimalsAutophagyBeclin-1Chlorocebus aethiopsCoronavirus InfectionsGene Knockdown TechniquesHEK293 CellsHumansMiddle East Respiratory Syndrome CoronavirusProteolysisS-Phase Kinase-Associated ProteinsUbiquitinationVero CellsBeclin-1BECN1 protein, humanSKP2 protein, humanS-Phase Kinase-Associated Proteins

Identifiers

PMID31852899
PMCPMC6920372
OpenAlexW2994840508

What Socratic 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 Socratic graph.