Evidence map›Paper›PMID 35080333›Full record

ArticleEMBO reports2022

USP17 is required for peripheral trafficking of lysosomes.

Jia Lin, Aidan P McCann, Naphannop Sereesongsaeng, Jonathan M Burden, Alhareth A Alsa'd, Roberta E Burden, Ileana Micu, Richard Williams, Sandra Van Schaeybroeck, Emma Evergren and 4 more

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2022. 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
1.0field-weighted citation impact, top 26% 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, 12 citations in OpenAlex.

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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

14 authors at 2 institutions in 2 countries.

Jia LinSchool of Pharmacy, Queen's University Belfast, Belfast, UK.
Aidan P McCannSchool of Pharmacy, Queen's University Belfast, Belfast, UK.
Naphannop SereesongsaengSchool of Pharmacy, Queen's University Belfast, Belfast, UK.
Jonathan M BurdenSchool of Pharmacy, Queen's University Belfast, Belfast, UK.
Alhareth A Alsa'dSchool of Pharmacy, Queen's University Belfast, Belfast, UK.
Roberta E BurdenSchool of Pharmacy, Queen's University Belfast, Belfast, UK.ORCID 0000-0002-3731-7939
Ileana MicuAdvanced Imaging Core Technology Unit, Faculty of Medicine, Health and Life Sciences, Queen's University Belfast, Belfast, UK.ORCID 0000-0001-7112-0075
Richard WilliamsPatrick G Johnston Centre for Cancer Research, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Belfast, UK.
Sandra Van SchaeybroeckPatrick G Johnston Centre for Cancer Research, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Belfast, UK.
Emma EvergrenPatrick G Johnston Centre for Cancer Research, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Belfast, UK.
Paul MullanPatrick G Johnston Centre for Cancer Research, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Belfast, UK.
Jeremy C SimpsonSchool of Biology and Environmental Science, UCD Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Dublin 4, Ireland.
Christopher J ScottPatrick G Johnston Centre for Cancer Research, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Belfast, UK.
James F BurrowsSchool of Pharmacy, Queen's University Belfast, Belfast, UK.ORCID 0000-0002-9677-200X
Queen's University Belfast · GBUniversity College Dublin · IE

Funding

Biotechnology and Biological Sciences Research Council BB/F013647/1
6 · The paper itself

Abstract

Expression of the deubiquitinase USP17 is induced by multiple stimuli, including cytokines (IL-4/6), chemokines (IL-8, SDF1), and growth factors (EGF), and several studies indicate it is required for cell proliferation and migration. However, the mechanisms via which USP17 impacts upon these cellular functions are unclear. Here, we demonstrate that USP17 depletion prevents peripheral lysosome positioning, as well as trafficking of lysosomes to the cell periphery in response to EGF stimulation. Overexpression of USP17 also increases secretion of the lysosomal protease cathepsin D. In addition, USP17 depletion impairs plasma membrane repair in cells treated with the pore-forming toxin streptolysin O, further indicating that USP17 is required for lysosome trafficking to the plasma membrane. Finally, we demonstrate that USP17 can deubiquitinate p62, and we propose that USP17 can facilitate peripheral lysosome trafficking by opposing the E3 ligase RNF26 to untether lysosomes from the ER and facilitate lysosome peripheral trafficking, lysosome protease secretion, and plasma membrane repair.

Indexed as

LysosomesCell MembraneCell ProliferationEGFexocytosislysosomeUSP17

Identifiers

PMID35080333
PMCPMC8982589
OpenAlexW4210307127

What OpenQuestion holds

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LicenceCC BY
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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.