Evidence map›Paper›PMID 11439104›Full record

ArticleThe Biochemical journal2001

Green fluorescent protein (GFP) tagged to the cytoplasmic tail of alphaIIb or beta3 allows the expression of a fully functional integrin alphaIIb(beta3): effect of beta3GFP on alphaIIb(beta3) ligand binding.

S Plançon, M C Morel-Kopp, E Schaffner-Reckinger, P Chen, N Kieffer

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 27% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Use of Ecto-Tagged Integrins to Monitor Integrin Exocytosis and Endocytosis.Methods in molecular biology (Clifton, N.J.) · 2023
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  7. Integrin-dependent force transmission to the extracellular matrix by α-actinin triggers adhesion maturation.Proceedings of the National Academy of Sciences of the United States of America · 2013
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  11. Review
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  13. Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering.Proceedings of the National Academy of Sciences of the United States of America · 2005
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  15. 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

5 authors.

S PlançonLaboratoire Franco-Luxembourgeois de Recherche Biomédicale (CNRS and CRP-Santé), Centre Universitaire, L-1511 Luxembourg, Grand-Duchy of Luxembourg.
M C Morel-Kopp
E Schaffner-Reckinger
P Chen
N Kieffer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Using green fluorescent protein (GFP) as an autofluorescent tag, we report the first successful visualization of a beta3 integrin in a living cell. GFP fused in frame to the cytoplasmic tail of either alphaIIb or beta3 allowed normal expression, heterodimerization, processing and surface exposure of alphaIIbGFPbeta3 and alphaIIb(beta3)GFP receptors in Chinese hamster ovary (CHO) cells. Direct microscopic observation of the autofluorescent cells in suspension following antibody-induced alphaIIb(beta3) capping revealed an intense autofluorescent cap corresponding to unlabelled immunoclustered GFP-tagged alphaIIb(beta3). GFP-tagged alphaIIbbeta3 receptors mediated fibrinogen-dependent cell adhesion, were readily detectable in focal adhesions of unstained living cells and triggered p125(FAK) tyrosine phosphorylation similar to wild-type alphaIIb(beta3) (where FAK corresponds to focal adhesion kinase). However, GFP tagged to beta3, but not to alphaIIb, induced spontaneous CHO cell aggregation in the presence of soluble fibrinogen, as well as binding of the fibrinogen mimetic monoclonal antibody PAC1 in the absence of alphaIIb(beta3) receptor activation. Time-lapse imaging of living transfectants revealed a characteristic redistribution of GFP-tagged alphaIIb(beta3) during the early stages of cell attachment and spreading, starting with alphaIIb(beta3) clustering at the rim of the cell contact area, that gradually overlapped with the boundary of the attached cell, and, with the onset of cell spreading, to a reorganization of alphaIIb(beta3) in focal adhesions. Taken together, our results demonstrate that (1) fusion of GFP to the cytoplasmic tail of either alphaIIb or beta3 integrin subunits allows normal cell surface expression of a functional receptor, and (2) structural modification of the beta3 integrin cytoplasmic tail, rather than the alphaIIb subunit, plays a major role in alphaIIb(beta3) affinity modulation. With the successful direct visualization of functional alphaIIb(beta3) receptors in living cells, the generation of autofluorescent integrins in transgenic animals will become possible, allowing new approaches to study the dynamics of integrin functions.

Indexed as

AnimalsAntigens, CDCell AdhesionCell AggregationCell MovementCHO CellsCricetinaeFibrinogenGenes, ReporterGreen Fluorescent ProteinsIntegrin beta3Luminescent ProteinsMicroscopy, VideoPlatelet Glycoprotein GPIIb-IIIa ComplexPlatelet Membrane GlycoproteinsPolymerase Chain ReactionAntigens, CDFibrinogenGreen Fluorescent ProteinsIntegrin beta3Luminescent ProteinsPlatelet Glycoprotein GPIIb-IIIa ComplexPlatelet Membrane GlycoproteinsRecombinant Fusion Proteins

Identifiers

PMID11439104
PMCPMC1221981
OpenAlexW164531134

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.