Evidence map›Paper›PMID 28820317›Full record

ArticleCell cycle (Georgetown, Tex.)2017

ULK1 ubiquitylation is regulated by phosphorylation on its carboxy terminus.

Francesca Nazio, Marianna Carinci, Francesco Cecconi

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. The Dawn of Mitophagy: What Do We Know by Now?Current neuropharmacology · 2021
    Review
  8. Article
  9. Roles of ubiquitin in autophagy and cell death.Seminars in cell & developmental biology · 2019
    Review
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

3 authors at 2 institutions in 2 countries.

Francesca Nazioa Department of Pediatric Hematology and Oncology , IRCSS Bambino Gesù Children's Hospital , Rome , Italy.ORCID http://orcid.org/0000-0002-3039-4448
Marianna Carincib Department of Biology , University of Rome Tor Vergata , Rome , Italy.ORCID http://orcid.org/0000-0001-8106-9656
Francesco Cecconia Department of Pediatric Hematology and Oncology , IRCSS Bambino Gesù Children's Hospital , Rome , Italy.ORCID http://orcid.org/0000-0002-5614-4359
University of Rome Tor Vergata · ITBambino Gesù Children's Hospital · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is a highly conserved process that acts sequestering cytoplasmic components for their degradation by the lysosomes. It consists of several sequential steps that have to be finely regulated to ensure both its progression and termination. Post-translational modifications (PTMs) play an important role in regulating ATG proteins function in different stages of autophagy. Recently, we demonstrated that, during prolonged starvation, ULK1 protein is specifically ubiquitylated by NEDD4L, and that this regulation is important to protect cells against excessive autophagy. In this Extra view, we show that ULK1 phosphorylation at 3 different sites on the same ULK1 target region for NEDD4L is preparatory for its ubiquitylation and subsequent degradation. This adds to the complexity of ULK1 multi-level regulation by several factors, including kinases, phosphatases and acetylases, with each contributing to autophagy homeostasis.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsAutophagyAutophagy-Related Protein-1 HomologHeLa CellsHumansIntracellular Signaling Peptides and ProteinsNedd4 Ubiquitin Protein LigasesPhosphorylationProteolysisSequestosome-1 ProteinUbiquitinationAutophagy-Related Protein-1 HomologIntracellular Signaling Peptides and ProteinsNedd4L protein, humanNedd4 Ubiquitin Protein LigasesSequestosome-1 ProteinSQSTM1 protein, humanULK1 protein, humanautophagykinasesubiquitinubiquitin ligases

Identifiers

PMID28820317
PMCPMC5628632
OpenAlexW2749865175

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.