Evidence map›Paper›PMID 33328309›Full record

ArticleJournal of virology2021

The Autophagy-Initiating Protein Kinase ULK1 Phosphorylates Human Cytomegalovirus Tegument Protein pp28 and Regulates Efficient Virus Release.

Patrick König, Adriana Svrlanska, Clarissa Read, Sabine Feichtinger, Thomas Stamminger

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2021. 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
1.6field-weighted citation impact, top 15% 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. Review
  2. Article
  3. The Autophagy ReceptorViruses · 2024
    Article
  4. Review
  5. Article
  6. The role of autophagy in viral infections.Journal of biomedical science · 2023
    Review
  7. Review
  8. Review
  9. Role of autophagy in gastric carcinogenesis.World journal of gastrointestinal oncology · 2021
    Review
  10. Review
  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

5 authors at 2 institutions in 1 country.

Patrick KönigInstitute of Virology, Ulm University Medical Center, Ulm, Germany.
Adriana SvrlanskaInstitute of Clinical and Molecular Virology, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.
Clarissa ReadInstitute of Virology, Ulm University Medical Center, Ulm, Germany.
Sabine Feichtinger *Institute of Clinical and Molecular Virology, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.
Thomas Stamminger *Institute of Virology, Ulm University Medical Center, Ulm, Germany thomas.stamminger@uniklinik-ulm.de.
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEUniversität Ulm · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is a catabolic process contributing to intrinsic cellular defense by degrading viral particles or proteins; however, several viruses hijack this pathway for their own benefit. The role of autophagy during human cytomegalovirus (HCMV) replication has not been definitely clarified yet. Utilizing small interfering RNA (siRNA)-based screening, we observed that depletion of many autophagy-related proteins resulted in reduced virus release, suggesting a requirement of autophagy-related factors for efficient HCMV replication. Additionally, we could show that the autophagy-initiating serine/threonine protein kinase ULK1 as well as other constituents of the ULK1 complex were upregulated at early times of infection and stayed upregulated throughout the replication cycle. We demonstrate that indirect interference with ULK1 through inhibition of the upstream regulator AMP-activated protein kinase (AMPK) impaired virus release. Furthermore, this result was verified by direct abrogation of ULK1 kinase activity utilizing the ULK1-specific kinase inhibitors SBI-0206965 and ULK-101. Analysis of viral protein expression in the presence of ULK-101 revealed a connection between the cellular kinase ULK1 and the viral tegument protein pp28 (pUL99), and we identified pp28 as a novel viral substrate of ULK1 by

Indexed as

Virus ReleaseAMP-Activated Protein KinasesAutophagyAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsCapsidCells, CulturedCytomegalovirusCytoplasmHumansIntracellular Signaling Peptides and ProteinsPhosphoproteinsPhosphorylationUp-RegulationViral Matrix ProteinsViral ProteinsAMP-Activated Protein KinasesAutophagy-Related Protein-1 HomologAutophagy-Related Proteinscytomegalovirus matrix protein 65kDahuman cytomegalovirus protein pp28Intracellular Signaling Peptides and ProteinsPhosphoproteinsULK1 protein, humanViral Matrix ProteinsViral Proteinsautophagyhuman cytomegalovirustegument proteinULK1

Identifiers

PMID33328309
PMCPMC8094963
OpenAlexW3111077917

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.