Evidence map›Paper›PMID 30924770›Full record

ArticleeLife2019

The homophilic receptor PTPRK selectively dephosphorylates multiple junctional regulators to promote cell-cell adhesion.

Gareth W Fearnley, Katherine A Young, James R Edgar, Robin Antrobus, Iain M Hay, Wei-Ching Liang, Nadia Martinez-Martin, WeiYu Lin, Janet E Deane, Hayley J Sharpe

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 42 citations in OpenAlex.

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  15. The progress of research into pseudophosphatases.Frontiers in public health · 2022
    Review
  16. Review
  17. Proximity-dependent labeling methods for proteomic profiling in living cells: An update.Wiley interdisciplinary reviews. Developmental biology · 2021
    Review
  18. Article
  19. Article
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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

10 authors at 1 institution in 1 country.

Gareth W FearnleyCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Katherine A YoungCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
James R EdgarCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0001-7903-8199
Robin AntrobusCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Iain M HayCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Wei-Ching LiangAntibody Engineering Department, Genentech, South San Francisco, United States.
Nadia Martinez-MartinMicrochemistry, Proteomics and Lipidomics Department, Genentech, South San Francisco, United States.
WeiYu LinAntibody Engineering Department, Genentech, South San Francisco, United States.
Janet E DeaneCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0002-4863-0330
Hayley J SharpeCambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0002-4723-298X
University of Cambridge · GB

Funding

Cancer Research UK PhD StudentshipRoyal Society 100371Wellcome 086598Wellcome and Royal Society Sir Henry Dale Fellowship: 109407Wellcome Trust
6 · The paper itself

Abstract

Cell-cell communication in multicellular organisms depends on the dynamic and reversible phosphorylation of protein tyrosine residues. The receptor-linked protein tyrosine phosphatases (RPTPs) receive cues from the extracellular environment and are well placed to influence cell signaling. However, the direct events downstream of these receptors have been challenging to resolve. We report here that the homophilic receptor PTPRK is stabilized at cell-cell contacts in epithelial cells. By combining interaction studies, quantitative tyrosine phosphoproteomics, proximity labeling and dephosphorylation assays we identify high confidence PTPRK substrates. PTPRK directly and selectively dephosphorylates at least five substrates, including Afadin, PARD3 and δ-catenin family members, which are all important cell-cell adhesion regulators. In line with this, loss of PTPRK phosphatase activity leads to disrupted cell junctions and increased invasive characteristics. Thus, identifying PTPRK substrates provides insight into its downstream signaling and a potential molecular explanation for its proposed tumor suppressor function.

Indexed as

Cell AdhesionProtein Processing, Post-TranslationalAdaptor Proteins, Signal TransducingCateninsCell Cycle ProteinsCell LineDelta CateninEpithelial CellsHumansMicrofilament ProteinsPhosphorylationReceptor-Like Protein Tyrosine Phosphatases, Class 2Adaptor Proteins, Signal TransducingafadinCateninsCell Cycle ProteinsDelta CateninMicrofilament ProteinsPARD3 protein, humanPTPRK protein, humanReceptor-Like Protein Tyrosine Phosphatases, Class 2cell biologycell-cell adhesiondephosphorylationhumanproteomicssignalingTyrosine phosphatase

Identifiers

PMID30924770
PMCPMC6440744
OpenAlexW2924149429

What OpenQuestion holds

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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.