Evidence map›Paper›PMID 32616830›Full record

ArticleScientific reports2020

ULK1 and ULK2 are less redundant than previously thought: computational analysis uncovers distinct regulation and functions of these autophagy induction proteins.

Amanda Demeter, Mari Carmen Romero-Mulero, Luca Csabai, Márton Ölbei, Padhmanand Sudhakar, Wilfried Haerty, Tamás Korcsmáros

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Autophagy · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Autophagy and cancer therapy.Cancer letters · 2024
    Review
  14. Article
  15. Article
  16. Physiological functions of ULK1/2.Journal of molecular biology · 2024
    Review
  17. Review
  18. Article
  19. Review
  20. 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

7 authors at 2 institutions in 3 countries.

Amanda DemeterEarlham Institute, Norwich Research Park, Norwich, NR4 7UZ, UK.
Mari Carmen Romero-MuleroEarlham Institute, Norwich Research Park, Norwich, NR4 7UZ, UK.
Luca CsabaiEarlham Institute, Norwich Research Park, Norwich, NR4 7UZ, UK.
Márton ÖlbeiEarlham Institute, Norwich Research Park, Norwich, NR4 7UZ, UK.
Padhmanand SudhakarEarlham Institute, Norwich Research Park, Norwich, NR4 7UZ, UK.
Wilfried HaertyEarlham Institute, Norwich Research Park, Norwich, NR4 7UZ, UK.
Tamás KorcsmárosEarlham Institute, Norwich Research Park, Norwich, NR4 7UZ, UK. Tamas.Korcsmaros@earlham.ac.uk.ORCID http://orcid.org/0000-0003-1717-996X
Norwich Research Park · GBEötvös Loránd University · HU

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
Biotechnology and Biological Sciences Research Council BBS/E/F/000PR10353Biotechnology and Biological Sciences Research Council BBS/E/F/000PR10355Medical Research Council MR/P026028/1NIGMS NIH HHS P41 GM103311
6 · The paper itself

Abstract

Macroautophagy, the degradation of cytoplasmic content by lysosomal fusion, is an evolutionary conserved process promoting homeostasis and intracellular defence. Macroautophagy is initiated primarily by a complex containing ULK1 or ULK2 (two paralogs of the yeast Atg1 protein). To understand the differences between ULK1 and ULK2, we compared the human ULK1 and ULK2 proteins and their regulation. Despite the similarity in their enzymatic domain, we found that ULK1 and ULK2 have major differences in their autophagy-related interactors and their post-translational and transcriptional regulators. We identified 18 ULK1-specific and 7 ULK2-specific protein motifs serving as different interaction interfaces. We found that interactors of ULK1 and ULK2 all have different tissue-specific expressions partially contributing to diverse and ULK-specific interaction networks in various tissues. We identified three ULK1-specific and one ULK2-specific transcription factor binding sites, and eight sites shared by the regulatory region of both genes. Importantly, we found that both their post-translational and transcriptional regulators are involved in distinct biological processes-suggesting separate functions for ULK1 and ULK2. Unravelling differences between ULK1 and ULK2 could lead to a better understanding of how ULK-type specific dysregulation affects autophagy and other cellular processes that have been implicated in diseases such as inflammatory bowel disease and cancer.

Indexed as

AutophagyAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsComputational BiologyHumansIntracellular Signaling Peptides and ProteinsLysosomesProtein BindingProtein ConformationProtein Interaction MappingProtein Serine-Threonine KinasesAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsIntracellular Signaling Peptides and ProteinsProtein Serine-Threonine KinasesULK1 protein, humanUlk2 protein, human

Identifiers

PMID32616830
PMCPMC7331686
OpenAlexW3040307105

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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.