Evidence map›Paper›PMID 29543760›Full record

ReviewCells2018

Receptor Tyrosine Kinase Ubiquitination and De-Ubiquitination in Signal Transduction and Receptor Trafficking.

William R Critchley, Caroline Pellet-Many, Benjamin Ringham-Terry, Michael A Harrison, Ian C Zachary, Sreenivasan Ponnambalam

Abstract readReview
In one paragraph

Review in Cells, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

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  19. Article
  20. Role of USP13 in physiology and diseases.Frontiers in molecular biosciences · 2022
    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

6 authors.

William R CritchleyEndothelial Cell Biology Unit, School of Molecular & Cellular Biology, University of Leeds, Leeds LS2 9JT, UK. w.r.critchley@leeds.ac.uk.
Caroline Pellet-ManyCentre for Cardiovascular Biology & Medicine, Rayne Building, University College London, London WC1E 6PT, UK. c.pellet-many@ucl.ac.uk.
Benjamin Ringham-TerryCentre for Cardiovascular Biology & Medicine, Rayne Building, University College London, London WC1E 6PT, UK. benjamin.ringham-terry@ucl.ac.uk.
Michael A HarrisonSchool of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, UK. m.a.harrison@leeds.ac.uk.ORCID 0000-0002-7826-7472
Ian C ZacharyCentre for Cardiovascular Biology & Medicine, Rayne Building, University College London, London WC1E 6PT, UK. i.zachary@ucl.ac.uk.
Sreenivasan PonnambalamEndothelial Cell Biology Unit, School of Molecular & Cellular Biology, University of Leeds, Leeds LS2 9JT, UK. s.ponnambalam@leeds.ac.uk.

Funding

British Heart Foundation PG/16/84/32464British Heart Foundation PG/16/86/32474British Heart Foundation RG/11/11/29050
6 · The paper itself

Abstract

Receptor tyrosine kinases (RTKs) are membrane-based sensors that enable rapid communication between cells and their environment. Evidence is now emerging that interdependent regulatory mechanisms, such as membrane trafficking, ubiquitination, proteolysis and gene expression, have substantial effects on RTK signal transduction and cellular responses. Different RTKs exhibit both basal and ligand-stimulated ubiquitination, linked to trafficking through different intracellular compartments including the secretory pathway, plasma membrane, endosomes and lysosomes. The ubiquitin ligase superfamily comprising the E1, E2 and E3 enzymes are increasingly implicated in this post-translational modification by adding mono- and polyubiquitin tags to RTKs. Conversely, removal of these ubiquitin tags by proteases called de-ubiquitinases (DUBs) enables RTK recycling for another round of ligand sensing and signal transduction. The endocytosis of basal and activated RTKs from the plasma membrane is closely linked to controlled proteolysis after trafficking and delivery to late endosomes and lysosomes. Proteolytic RTK fragments can also have the capacity to move to compartments such as the nucleus and regulate gene expression. Such mechanistic diversity now provides new opportunities for modulating RTK-regulated cellular responses in health and disease states.

Indexed as

de-ubiquitinasesproteolysisreceptor tyrosine kinasessignal transductiontraffickingubiquitinubiquitin ligases

Identifiers

PMID29543760
PMCPMC5870354

What Socratic 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 Socratic graph.