Evidence map›Paper›PMID 29563162›Full record

ArticleBioscience reports2018

mTOR independent alteration in ULK1 Ser758 phosphorylation following chronic LRRK2 kinase inhibition.

Claudia Manzoni, Adamantios Mamais, Sybille Dihanich, Marc P M Soutar, Helene Plun-Favreau, Rina Bandopadhyay, Rosella Abeti, Paola Giunti, John Hardy, Mark R Cookson and 2 more

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2018. 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
1.1field-weighted citation impact, top 27% 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. Review
  3. Review
  4. Article
  5. Review
  6. "LRRK2: Autophagy and Lysosomal Activity".Frontiers in neuroscience · 2020
    Review
  7. Article
  8. Autophagy and LRRK2 in the Aging Brain.Frontiers in neuroscience · 2019
    Review
  9. Review
  10. Article
  11. 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

12 authors at 1 institution in 1 country.

Claudia ManzoniSchool of Pharmacy, University of Reading, Whiteknights, Reading RG6 6AP, U.K. c.manzoni@reading.ac.uk.
Adamantios MamaisLaboratory of Neurogenetics, National Institute on Aging, National Institutes of Health, Bethesda, MD 20892, U.S.A.
Sybille DihanichDepartment of Molecular Neuroscience, UCL Institute of Neurology, Queen Square, London WC1N 3BG, U.K.
Marc P M SoutarDepartment of Molecular Neuroscience, UCL Institute of Neurology, Queen Square, London WC1N 3BG, U.K.
Helene Plun-FavreauDepartment of Molecular Neuroscience, UCL Institute of Neurology, Queen Square, London WC1N 3BG, U.K.
Rina BandopadhyayReta Lila Weston Institute of Neurological Studies, UCL Institute of Neurology, 1 Wakefield Street London WC1N 1PJ, U.K.
Rosella AbetiDepartment of Molecular Neuroscience, UCL Institute of Neurology, Queen Square, London WC1N 3BG, U.K.
Paola GiuntiDepartment of Molecular Neuroscience, UCL Institute of Neurology, Queen Square, London WC1N 3BG, U.K.
John HardyDepartment of Molecular Neuroscience, UCL Institute of Neurology, Queen Square, London WC1N 3BG, U.K.
Mark R CooksonLaboratory of Neurogenetics, National Institute on Aging, National Institutes of Health, Bethesda, MD 20892, U.S.A.
Sharon A ToozeThe Francis Crick Institute, 1 Midland Road, London, NW1 1AT, U.K.
Patrick A LewisSchool of Pharmacy, University of Reading, Whiteknights, Reading RG6 6AP, U.K.
The Francis Crick Institute · GB

Funding

Cancer Research UK FC001187Medical Research Council MR/L010933/1Medical Research Council MR/N026004/1Wellcome Trust WT089698
6 · The paper itself

Abstract

Unc-51 Like Kinase 1 (ULK1) is a critical regulator of the biogenesis of autophagosomes, the central component of the catabolic macroautophagy pathway. Regulation of ULK1 activity is dependent upon several phosphorylation events acting to repress or activate the enzymatic function of this protein. Phosphorylation of Ser758 ULK1 has been linked to repression of autophagosome biogenesis and was thought to be exclusively dependent upon mTOR complex 1 kinase activity. In the present study, a novel regulation of Ser758 ULK1 phosphorylation is reported following prolonged inhibition of the Parkinson's disease linked protein leucine rich repeat kinase 2 (LRRK2). Here, modulation of Ser758 ULK1 phosphorylation following LRRK2 inhibition is decoupled from the repression of autophagosome biogenesis and independent of mTOR complex 1 activity.

Indexed as

AnimalsAutophagosomesAutophagy-Related Protein-1 HomologCell LineLeucine-Rich Repeat Serine-Threonine Protein Kinase-2Mechanistic Target of Rapamycin Complex 1PhosphorylationRatsSerineTOR Serine-Threonine KinasesAutophagy-Related Protein-1 HomologLeucine-Rich Repeat Serine-Threonine Protein Kinase-2LRRK2 protein, ratMechanistic Target of Rapamycin Complex 1mTOR protein, ratSerineTOR Serine-Threonine KinasesULK1 protein, ratautophagycancerLeucin Rich Repeat Kinase 2 (LRRK2)mammalian Target Of Rapamycin (mTOR)Parkinson diseaseUnc-51 Like Kinase 1 (ULK1)

Identifiers

PMID29563162
PMCPMC5968188
OpenAlexW2793336576

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.