Evidence map›Paper›PMID 11401727›Full record

ArticleBMC cell biology2001

Dimerization of receptor protein-tyrosine phosphatase alpha in living cells.

L G Tertoolen, C Blanchetot, G Jiang, J Overvoorde, T W Gadella, T Hunter, J den Hertog

Open access · goldAbstract read
In one paragraph

Article in BMC cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 92 citations in OpenAlex.

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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

7 authors at 4 institutions in 2 countries.

L G TertoolenHubrecht Laboratory, Netherlands Institute for Developmental Biology, Utrecht, The Netherlands. leon@niob.knaw.nl
C Blanchetot
G Jiang
J Overvoorde
T W Gadella
T Hunter
J den Hertog
Hubrecht Institute for Developmental Biology and Stem Cell Research · NLMerck & Co., Inc., Rahway, NJ, USA (United States) · USSalk Institute for Biological Studies · USWageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundDimerization is an important regulatory mechanism of single membrane-spanning receptors. For instance, activation of receptor protein-tyrosine kinases (RPTKs) involves dimerization. Structural, functional and biochemical studies suggested that the enzymatic counterparts of RPTKs, the receptor protein-tyrosine phosphatases (RPTPs), are inhibited by dimerization, but whether RPTPs actually dimerize in living cells remained to be determined.

resultsIn order to assess RPTP dimerization, we have assayed Fluorescence Resonance Energy Transfer (FRET) between chimeric proteins of cyan- and yellow-emitting derivatives of green fluorescent protein, fused to RPTPalpha, using three different techniques: dual wavelength excitation, spectral imaging and fluorescence lifetime imaging. All three techniques suggested that FRET occurred between RPTPalpha -CFP and -YFP fusion proteins, and thus that RPTPalpha dimerized in living cells. RPTPalpha dimerization was constitutive, extensive and specific. RPTPalpha dimerization was consistent with cross-linking experiments, using a non-cell-permeable chemical cross-linker. Using a panel of deletion mutants, we found that the transmembrane domain was required and sufficient for dimerization.

conclusionsWe demonstrate here that RPTPalpha dimerized constitutively in living cells, which may be mediated by the transmembrane domain, providing strong support for the model that dimerization is involved in regulation of RPTPs.

Indexed as

Receptors, Cell SurfaceCross-Linking ReagentsDimerizationEnergy TransferFluorescenceGreen Fluorescent ProteinsLuminescent ProteinsMicroscopy, FluorescenceProtein Structure, TertiaryProtein Tyrosine PhosphatasesReceptor-Like Protein Tyrosine Phosphatases, Class 4Recombinant Fusion ProteinsSpectrometry, FluorescenceTumor Cells, CulturedCross-Linking ReagentsGreen Fluorescent ProteinsLuminescent ProteinsProtein Tyrosine PhosphatasesReceptor-Like Protein Tyrosine Phosphatases, Class 4Receptors, Cell SurfaceRecombinant Fusion Proteins

Identifiers

PMID11401727
PMCPMC32300
OpenAlexW2120750481

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.