Evidence map›Paper›PMID 21135139›Full record

ArticleThe Journal of cell biology2010

PTP1B regulates Eph receptor function and trafficking.

Eva Nievergall, Peter W Janes, Carolin Stegmayer, Mary E Vail, Fawaz G Haj, Shyh Wei Teng, Benjamin G Neel, Philippe I Bastiaens, Martin Lackmann

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Protein-tyrosine phosphatase 1B substrates and metabolic regulation.Seminars in cell & developmental biology · 2015
    Review
  12. Eph- and ephrin-dependent mechanisms in tumor and stem cell dynamics.Cellular and molecular life sciences : CMLS · 2014
    Review
  13. Article
  14. Article
  15. Tie2 and Eph receptor tyrosine kinase activation and signaling.Cold Spring Harbor perspectives in biology · 2014
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Therapeutic targeting of EPH receptors and their ligands.Nature reviews. Drug discovery · 2014
    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

9 authors at 5 institutions in 4 countries.

Eva NievergallDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
Peter W Janes
Carolin Stegmayer
Mary E Vail
Fawaz G Haj
Shyh Wei Teng
Benjamin G Neel
Philippe I Bastiaens
Martin Lackmann
Institute of Molecular Biology and Biophysics · RUBeth Israel Deaconess Medical Center · USHarvard University · USMax Planck Institute of Molecular Physiology · DEMonash University · AU

Funding

Signal Transduction by Non-transmembrane PTPsR37CA049152 · NCI · UNIVERSITY HEALTH NETWORK · PI NEEL, BENJAMIN G. · 2004 to 2013
$4.0M
NCI NIH HHS R37 CA049152NCI NIH HHS R37 CA49152
6 · The paper itself

Abstract

Eph receptors orchestrate cell positioning during normal and oncogenic development. Their function is spatially and temporally controlled by protein tyrosine phosphatases (PTPs), but the underlying mechanisms are unclear and the identity of most regulatory PTPs are unknown. We demonstrate here that PTP1B governs signaling and biological activity of EphA3. Changes in PTP1B expression significantly affect duration and amplitude of EphA3 phosphorylation and biological function, whereas confocal fluorescence lifetime imaging microscopy (FLIM) reveals direct interactions between PTP1B and EphA3 before ligand-stimulated receptor internalization and, subsequently, on endosomes. Moreover, overexpression of wild-type (w/t) PTP1B and the [D-A] substrate-trapping mutant decelerate ephrin-induced EphA3 trafficking in a dose-dependent manner, which reveals its role in controlling EphA3 cell surface concentration. Furthermore, we provide evidence that in areas of Eph/ephrin-mediated cell-cell contacts, the EphA3-PTP1B interaction can occur directly at the plasma membrane. Our studies for the first time provide molecular, mechanistic, and functional insights into the role of PTP1B controlling Eph/ephrin-facilitated cellular interactions.

Indexed as

Cell MembraneCells, CulturedHumansMicroscopy, ConfocalProtein Tyrosine Phosphatase, Non-Receptor Type 1Receptor, EphA1Protein Tyrosine Phosphatase, Non-Receptor Type 1Receptor, EphA1

Identifiers

PMID21135139
PMCPMC3002030
OpenAlexW2138999412

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.