Evidence map›Paper›PMID 19573017›Full record

ArticleJournal of neurochemistry2009

Dimerization of tyrosine phosphatase PTPRO decreases its activity and ability to inactivate TrkC.

Amy E Hower, Pedro J Beltran, John L Bixby

Abstract readComparative Study
In one paragraph

Article in Journal of neurochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. A C-terminal nonsense mutation links PTPRQ with autosomal-dominant hearing loss, DFNA73.Genetics in medicine : official journal of the American College of Medical Genetics · 2018
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Protein tyrosine phosphatase receptor type O inhibits trigeminal axon growth and branching by repressing TrkB and Ret signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  13. Review
  14. Article
  15. Thrombospondin-1 acts as a ligand for CD148 tyrosine phosphatase.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  16. Inside the human cancer tyrosine phosphatome.Nature reviews. Cancer · 2011
    Review
  17. 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

3 authors at 1 institution in 1 country.

Amy E HowerProgram in Neuroscience, University of Miami, Miami, Florida 33136, USA.
Pedro J Beltran
John L Bixby
University of Miami · US

Funding

RPTPs in the Growth of Vertebrate AxonsR01NS038920 · NINDS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BIXBY, JOHN L · 1999 to 2008
$2.6M
NINDS NIH HHS NS38920NINDS NIH HHS R01 NS038920
6 · The paper itself

Abstract

Receptor-protein tyrosine phosphatases (RPTPs), like receptor tyrosine kinases, regulate neuronal differentiation. While receptor tyrosine kinases are dimerized and activated by extracellular ligands, the extent to which RPTPs dimerize, and the effects of dimerization on phosphatase activity, are poorly understood. We have examined a neuronal type III RPTP, PTPRO; we find that PTPRO can form dimers in living cells, and that disulfide linkages in PTPROs intracellular domain likely regulate dimerization. Dimerization of PTPROs transmembrane and intracellular domains, achieved by ligand binding to a chimeric fusion protein, decreases activity toward artificial peptides and toward a putative substrate, tropomyosin-related kinase C (TrkC). Dephosphorylation of TrkC by PTPRO may be physiologically relevant, as it is efficient, and TrkC and PTPRO can be co-precipitated from transfected cells. Inhibition of PTPROs phosphatase activity by dimerization is interesting, as dimerization of a related RPTP, CD148/PTPRJ, increases activity. Thus, our results suggest a complex relationship between dimerization and activity in type III RPTPs.

Indexed as

Protein MultimerizationAnimalsChickensChlorocebus aethiopsCOS CellsDisulfidesEnzyme ActivationHumansHydrogen BondingMiceMice, KnockoutMutagenesis, Site-DirectedMutant Chimeric ProteinsProtein Structure, TertiaryReceptor-Like Protein Tyrosine Phosphatases, Class 3Receptor, trkCDisulfidesMutant Chimeric ProteinsPTPRO protein, humanReceptor-Like Protein Tyrosine Phosphatases, Class 3Receptor, trkC

Identifiers

PMID19573017
PMCPMC13521113
OpenAlexW2041622297

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.