Evidence map›Paper›PMID 21876762›Full record

ArticlePloS one2011

TC-PTP dephosphorylates the guanine nucleotide exchange factor C3G (RapGEF1) and negatively regulates differentiation of human neuroblastoma cells.

Aninda Mitra, Srinivasan Kalayarasan, Vijay Gupta, Vegesna Radha

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Identification of Protein Tyrosine Phosphatase (PTP) Substrates.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  3. Review
  4. Article
  5. C3G Protein, a New Player in Glioblastoma.International journal of molecular sciences · 2021
    Review
  6. Article
  7. Review
  8. Article
  9. 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

4 authors at 2 institutions in 1 country.

Aninda MitraCentre for Cellular and Molecular Biology, Council of Scientific and Industrial Research, Hyderabad, Andhra Pradesh, India.
Srinivasan Kalayarasan
Vijay Gupta
Vegesna Radha
Council of Scientific and Industrial Research · INCentre for Cellular and Molecular Biology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The guanine nucleotide exchange factor, C3G (RapGEF1), functions in multiple signaling pathways involved in cell adhesion, proliferation, apoptosis and actin reorganization. C3G is regulated by tyrosine phosphorylation on Y504, known to be mediated by c-Abl and Src family kinases. In the present study we explored the possibility of cellular phospho-C3G (pC3G) being a substrate of the intracellular T-cell protein tyrosine phosphatase TC-PTP (PTPN2) using the human neuroblastoma cell line, IMR-32. In vivo and in vitro binding assays demonstrated interaction between C3G and TC-PTP. Interaction is mediated through the Crk-binding region of C3G and C-terminal noncatalytic residues of TC-PTP. C3G interacted better with a substrate trap mutant of TC48 and this complex formation was inhibited by vanadate. Endogenous pC3G colocalized with catalytically inactive mutant TC48 in the Golgi. Expression of TC48 abrogated pervanadate and c-Src induced phosphorylation of C3G without affecting total cellular phospho-tyrosine. Insulin-like growth factor treatment of c-Src expressing cells resulted in dephosphorylation of C3G dependent on the activity of endogenous TC48. TC48 expression inhibited forskolin induced tyrosine phosphorylation of C3G and neurite outgrowth in IMR-32 cells. Our results identify a novel Golgi localized substrate of TC48 and delineate a role for TC48 in dephosphorylation of substrates required during differentiation of human neuroblastoma cells.

Indexed as

Cell DifferentiationCell Line, TumorColforsinGolgi ApparatusGuanine Nucleotide-Releasing Factor 2HEK293 CellsHumansMutant ProteinsNeuritesNeuroblastomaPhosphorylationPhosphotyrosineProtein BindingProtein Structure, TertiaryProtein TransportProtein Tyrosine Phosphatase, Non-Receptor Type 2ColforsinGuanine Nucleotide-Releasing Factor 2Mutant ProteinspervanadatePhosphotyrosineProtein Tyrosine Phosphatase, Non-Receptor Type 2PTPN2 protein, humansrc-Family KinasesVanadates

Identifiers

PMID21876762
PMCPMC3158094
OpenAlexW2082538976

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.