Evidence map›Paper›PMID 28740133›Full record

ArticleNature communications2017

Spatial cycles mediated by UNC119 solubilisation maintain Src family kinases plasma membrane localisation.

Antonios D Konitsiotis, Lisaweta Roßmannek, Angel Stanoev, Malte Schmick, Philippe I H Bastiaens

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. 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
2.8field-weighted citation impact, top 10% 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, 31 citations in OpenAlex.

  1. The Arf family GTPases: Regulation of vesicle biogenesis and beyond.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
  2. Article
  3. Review
  4. Understanding Ras Spatial Cycles Through Reaction-Diffusion Simulations.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  5. TASK channels: channelopathies, trafficking, and receptor-mediated inhibition.Pflugers Archiv : European journal of physiology · 2020
    Review
  6. Article
  7. Article
  8. Serine/Threonine Protein Kinase STK16.International journal of molecular sciences · 2019
    Review
  9. Article
  10. Article
  11. Article
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

5 authors at 2 institutions in 1 country.

Antonios D KonitsiotisDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany.
Lisaweta RoßmannekDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany.
Angel StanoevDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany.
Malte SchmickDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany.
Philippe I H BastiaensDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany. philippe.bastiaens@mpi-dortmund.mpg.de.
Max Planck Institute of Molecular Physiology · DETU Dortmund University · DE

Funding

European Research Council 322637
6 · The paper itself

Abstract

The peripheral membrane proto-oncogene Src family protein tyrosine kinases relay growth factor signals to the cytoplasm of mammalian cells. We unravel the spatial cycles of solubilisation, trapping on perinuclear membrane compartments and vesicular transport that counter entropic equilibration to endomembranes for maintaining the enrichment and activity of Src family protein tyrosine kinases at the plasma membrane. The solubilising factor UNC119 sequesters myristoylated Src family protein tyrosine kinases from the cytoplasm, enhancing their diffusion to effectively release Src family protein tyrosine kinases on the recycling endosome by localised Arl2/3 activity. Src is then trapped on the recycling endosome via electrostatic interactions, whereas Fyn is quickly released to be kinetically trapped on the Golgi by palmitoyl acyl-transferase activity. Vesicular trafficking from these compartments restores enrichment of the Src family protein tyrosine kinases to the plasma membrane. Interference with these spatial cycles by UNC119 knockdown disrupts Src family protein tyrosine kinase localisation and signalling activity, indicating that UNC119 could be a drug target to affect oncogenic Src family protein tyrosine kinase signalling.The peripheral membrane proto-oncogene Src family protein tyrosine kinases (SFKs) transmit growth factor signals to the cytoplasm. Here the authors show that the solubilising factor UNC119 sequesters myristoylated SFKs to maintain its enrichment at the plasma membrane to enable signal transduction.

Indexed as

Signal TransductionAdaptor Proteins, Signal TransducingADP-Ribosylation FactorsCell LineCell MembraneEndosomesGolgi ApparatusGTP-Binding ProteinsHeLa CellsHT29 CellsHumansImmunoblottingMicroscopy, ConfocalModels, BiologicalMyristic AcidProtein BindingAdaptor Proteins, Signal TransducingADP-Ribosylation FactorsARL2 protein, humanARL3 protein, humanGTP-Binding ProteinsMAS1 protein, humanMyristic AcidProto-Oncogene MasProto-Oncogene Proteins c-fynsrc-Family KinasesUNC119 protein, human

Identifiers

PMID28740133
PMCPMC5524651
OpenAlexW2735468098

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.