Evidence map›Paper›PMID 31733992›Full record

ArticleMolecular cell2020

An mTORC1-to-CDK1 Switch Maintains Autophagy Suppression during Mitosis.

Richard I Odle, Simon A Walker, David Oxley, Andrew M Kidger, Kathryn Balmanno, Rebecca Gilley, Hanneke Okkenhaug, Oliver Florey, Nicholas T Ktistakis, Simon J Cook

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
8.5field-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

63 citing papers in PubMed, 113 citations in OpenAlex.

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  17. Physiological functions of ULK1/2.Journal of molecular biology · 2024
    Review
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  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Richard I OdleSignalling Laboratory, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK. Electronic address: richard.odle@babraham.ac.uk.
Simon A WalkerImaging Facility, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
David OxleyProteomics Facility, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Andrew M KidgerSignalling Laboratory, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Kathryn BalmannoSignalling Laboratory, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Rebecca GilleySignalling Laboratory, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Hanneke OkkenhaugImaging Facility, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Oliver FloreySignalling Laboratory, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Nicholas T KtistakisSignalling Laboratory, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Simon J CookSignalling Laboratory, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK. Electronic address: simon.cook@babraham.ac.uk.
Babraham Institute · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K019155/1Biotechnology and Biological Sciences Research Council BBS/E/B/000C0413Biotechnology and Biological Sciences Research Council BBS/E/B/000C0417Cancer Research UK 16337
6 · The paper itself

Abstract

Since nuclear envelope breakdown occurs during mitosis in metazoan cells, it has been proposed that macroautophagy must be inhibited to maintain genome integrity. However, repression of macroautophagy during mitosis remains controversial and mechanistic detail limited to the suggestion that CDK1 phosphorylates VPS34. Here, we show that initiation of macroautophagy, measured by the translocation of the ULK complex to autophagic puncta, is repressed during mitosis, even when mTORC1 is inhibited. Indeed, mTORC1 is inactive during mitosis, reflecting its failure to localize to lysosomes due to CDK1-dependent RAPTOR phosphorylation. While mTORC1 normally represses autophagy via phosphorylation of ULK1, ATG13, ATG14, and TFEB, we show that the mitotic phosphorylation of these autophagy regulators, including at known repressive sites, is dependent on CDK1 but independent of mTOR. Thus, CDK1 substitutes for inhibited mTORC1 as the master regulator of macroautophagy during mitosis, uncoupling autophagy regulation from nutrient status to ensure repression of macroautophagy during mitosis.

Indexed as

A549 CellsAutophagyCDC2 Protein KinaseCell LineCell Line, TumorFemaleHCT116 CellsHEK293 CellsHeLa CellsHT29 CellsHumansLysosomesMaleMechanistic Target of Rapamycin Complex 1MitosisPhosphorylationCDC2 Protein KinaseCDK1 protein, humanMechanistic Target of Rapamycin Complex 1ATG13ATG14autophagyCDK1mitosismTORRAPTORTFEBULK1

Identifiers

PMID31733992
PMCPMC6964153
OpenAlexW2987304637

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.