Evidence map›Paper›PMID 27557622›Full record

ArticleJournal of cell science2016

Exosomes bind to autotaxin and act as a physiological delivery mechanism to stimulate LPA receptor signalling in cells.

Susanna A Jethwa, Emma J Leah, Qifeng Zhang, Nicholas A Bright, David Oxley, Martin D Bootman, Simon A Rudge, Michael J O Wakelam

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 49 citations in OpenAlex.

  1. G protein-coupled receptors: a gateway to targeting oncogenic EVs?Extracellular vesicles and circulating nucleic acids · 2024
    Review
  2. Review
  3. Review
  4. Article
  5. Design and Development of Autotaxin Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Calcium Signaling and Tissue Calcification.Cold Spring Harbor perspectives in biology · 2019
    Review
  18. Emerging structural biology of lipid G protein-coupled receptors.Protein science : a publication of the Protein Society · 2019
    Review
  19. Frontiers in immunology · 2019
    Review
  20. 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

8 authors at 2 institutions in 1 country.

Susanna A JethwaBabraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Emma J LeahBabraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Qifeng ZhangBabraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Nicholas A BrightCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK.
David OxleyBabraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Martin D BootmanBabraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Simon A RudgeBabraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK Simon.rudge@babraham.ac.uk Michael.wakelam@babraham.ac.uk.
Michael J O WakelamBabraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK Simon.rudge@babraham.ac.uk Michael.wakelam@babraham.ac.uk.ORCID 0000-0003-4059-9276
Babraham Institute · GBUniversity of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/B/000C0415
6 · The paper itself

Abstract

Autotaxin (ATX; also known as ENPP2), the lysophospholipase responsible for generating the lipid receptor agonist lysophosphatidic acid (LPA), is a secreted enzyme. Here we show that, once secreted, ATX can bind to the surface of cell-secreted exosomes. Exosome-bound ATX is catalytically active and carries generated LPA. Once bound to a cell, through specific integrin interactions, ATX releases the LPA to activate cell surface G-protein-coupled receptors of LPA; inhibition of signalling by the receptor antagonist Ki1642 suggests that these receptors are LPAR1 and LPAR3. The binding stimulates downstream signalling, including phosphorylation of AKT and mitogen-activated protein kinases, the release of intracellular stored Ca

Indexed as

Signal TransductionAnimalsCentrifugation, Density GradientChemical FractionationCulture Media, ConditionedDNAExosomesHEK293 CellsHumansLamininLysophospholipase DLysophospholipidsMass SpectrometryMiceMultivesicular BodiesNIH 3T3 CellsCulture Media, ConditionedDNALamininLysophospholipase DLysophospholipidsPhosphoric Diester HydrolasesReceptors, Lysophosphatidic AcidAutotaxinExosomeIntegrinLPA

Identifiers

PMID27557622
PMCPMC5087657
OpenAlexW2513477456

What OpenQuestion holds

Textmetadata
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.