Evidence map›Paper›PMID 28499815›Full record

ArticleBiochimica et biophysica acta. Molecular and cell biology of lipids2017

New insight into the interaction of TRAF2 C-terminal domain with lipid raft microdomains.

Arianna Ceccarelli, Almerinda Di Venere, Eleonora Nicolai, Anastasia De Luca, Nicola Rosato, Enrico Gratton, Giampiero Mei, Anna Maria Caccuri

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Molecular and cell biology of lipids, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

  1. Structural dynamics and pH-regulated membrane binding of the TRAF2-NC trimer.Protein science : a publication of the Protein Society · 2026
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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

8 authors at 3 institutions in 2 countries.

Arianna CeccarelliDepartment of Experimental Medicine and Surgery, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy.
Almerinda Di VenereDepartment of Experimental Medicine and Surgery, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy; Center NAST, Nanoscience, Nanotechnology, Innovative Instrumentation, University of Rome Tor Vergata, 00133 Rome, Italy.
Eleonora NicolaiDepartment of Experimental Medicine and Surgery, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy.
Anastasia De LucaDepartment of Experimental Medicine and Surgery, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy.
Nicola RosatoDepartment of Experimental Medicine and Surgery, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy; Center NAST, Nanoscience, Nanotechnology, Innovative Instrumentation, University of Rome Tor Vergata, 00133 Rome, Italy.
Enrico GrattonLaboratory for Fluorescence Dynamics, Biomedical Engineering Department, University of California at Irvine, Irvine, CA, USA.
Giampiero MeiDepartment of Experimental Medicine and Surgery, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy; Center NAST, Nanoscience, Nanotechnology, Innovative Instrumentation, University of Rome Tor Vergata, 00133 Rome, Italy. Electronic address: mei@med.uniroma2.it.
Anna Maria CaccuriDepartment of Experimental Medicine and Surgery, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy; Center NAST, Nanoscience, Nanotechnology, Innovative Instrumentation, University of Rome Tor Vergata, 00133 Rome, Italy. Electronic address: caccuri@uniroma2.it.
University of Rome Tor Vergata · ITInnova (Italy) · ITFluor (United States) · US

Funding

Uncover Strategies Used By Biological SystemsP50GM076516 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI NIE, QING · 2007 to 2016
$25.1M
TRD4: Phasor analysisP41GM103540 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI GRATTON, ENRICO · 2012 to 2020
$12.5M
NIGMS NIH HHS P41 GM103540NIGMS NIH HHS P50 GM076516
6 · The paper itself

Abstract

In this study we provide the first evidence of the interaction of a truncated-TRAF2 with lipid raft microdomains. We have analyzed this interaction by measuring the diffusion coefficient of the protein in large and giant unilamellar vesicles (LUVs and GUVs, respectively) obtained both from synthetic lipid mixtures and from natural extracts. Steady-state fluorescence measurements performed with synthetic vesicles indicate that this truncated form of TRAF2 displays a tighter binding to raft-like LUVs with respect to the control (POPC-containing LUVs), and that this process depends on the protein oligomeric state. Generalized Polarization measurements and spectral phasor analysis revealed that truncated-TRAF2 affects the membrane fluidity, especially when vesicles are heated up at physiological temperature. The addition of nanomolar concentration of TRAF2 in GUVs also seems to exert a mechanical action, as demonstrated by the formation of intraluminal vesicles, a process in which ganglioside GM1 plays a crucial role.

Indexed as

DiffusionFluorescenceG(M1) GangliosideHumansLipid BilayersLipidsMembrane FluidityMembrane MicrodomainsProtein BindingProtein DomainsTNF Receptor-Associated Factor 2Unilamellar LiposomesG(M1) GangliosideLipid BilayersLipidsPSMD2 protein, humanTNF Receptor-Associated Factor 2Unilamellar LiposomesFluorescence microscopyGeneral PolarizationLipid raftsProtein–lipid interaction

Identifiers

PMID28499815
PMCPMC5562040
OpenAlexW2613686986

What OpenQuestion holds

Textmetadata
LicenceTDM
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.