CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse

Regina Tavano, Rita Lucia Contento, Sonia Jimenez Baranda, Marzia Soligo, Loretta Tuosto, Santos Manes, Antonella Viola

Research output: Contribution to journalArticle

111 Citations (Scopus)

Abstract

During physiological T-cell stimulation by antigen presenting cells (APCs), a major T-cell membrane rearrangement is known to occur leading to the organization of 'supramolecular activation clusters' at the immunological synapse1,2. A possible role for the synapse is the generation of membrane compartments where signalling may be organized and propagated2. Thus, engagement of the costimulatory molecule CD28 at the immunological synapse promotes the organization of a signalling compartment by inducing cytoskeletal changes and lipid raft accumulation3-5. We identified the actin-binding protein Filamin-A (FLNa) as a novel molecular partner of CD28. We found that, after physiological stimulation, CD28 associated with and recruited FLNa into the immunological synapse, where FLNa organized CD28 signalling. FLNa knockdown by short interfering RNA (siRNA) inhibited CD28-mediated raft accumulation at the immunological synapse and T-cell costimulation. Together, our data indicate that CD28 binding to FLNa is required to induce the T-cell cytoskeletal rearrangements leading to recruitment of lipid microdomains and signalling mediators into the immunological synapse.

Original languageEnglish
Pages (from-to)1270-1276
Number of pages7
JournalNature Cell Biology
Volume8
Issue number11
DOIs
Publication statusPublished - Nov 2006

Fingerprint

Immunological Synapses
Filamins
T-Lymphocytes
Lipids
Microfilament Proteins
Antigen-Presenting Cells
Synapses
Small Interfering RNA
Cell Membrane
Membranes

ASJC Scopus subject areas

  • Cell Biology

Cite this

Tavano, R., Contento, R. L., Baranda, S. J., Soligo, M., Tuosto, L., Manes, S., & Viola, A. (2006). CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse. Nature Cell Biology, 8(11), 1270-1276. https://doi.org/10.1038/ncb1492

CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse. / Tavano, Regina; Contento, Rita Lucia; Baranda, Sonia Jimenez; Soligo, Marzia; Tuosto, Loretta; Manes, Santos; Viola, Antonella.

In: Nature Cell Biology, Vol. 8, No. 11, 11.2006, p. 1270-1276.

Research output: Contribution to journalArticle

Tavano, R, Contento, RL, Baranda, SJ, Soligo, M, Tuosto, L, Manes, S & Viola, A 2006, 'CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse', Nature Cell Biology, vol. 8, no. 11, pp. 1270-1276. https://doi.org/10.1038/ncb1492
Tavano R, Contento RL, Baranda SJ, Soligo M, Tuosto L, Manes S et al. CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse. Nature Cell Biology. 2006 Nov;8(11):1270-1276. https://doi.org/10.1038/ncb1492
Tavano, Regina ; Contento, Rita Lucia ; Baranda, Sonia Jimenez ; Soligo, Marzia ; Tuosto, Loretta ; Manes, Santos ; Viola, Antonella. / CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse. In: Nature Cell Biology. 2006 ; Vol. 8, No. 11. pp. 1270-1276.
@article{a69f2ff19a5845629b8e604bc85d0c5f,
title = "CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse",
abstract = "During physiological T-cell stimulation by antigen presenting cells (APCs), a major T-cell membrane rearrangement is known to occur leading to the organization of 'supramolecular activation clusters' at the immunological synapse1,2. A possible role for the synapse is the generation of membrane compartments where signalling may be organized and propagated2. Thus, engagement of the costimulatory molecule CD28 at the immunological synapse promotes the organization of a signalling compartment by inducing cytoskeletal changes and lipid raft accumulation3-5. We identified the actin-binding protein Filamin-A (FLNa) as a novel molecular partner of CD28. We found that, after physiological stimulation, CD28 associated with and recruited FLNa into the immunological synapse, where FLNa organized CD28 signalling. FLNa knockdown by short interfering RNA (siRNA) inhibited CD28-mediated raft accumulation at the immunological synapse and T-cell costimulation. Together, our data indicate that CD28 binding to FLNa is required to induce the T-cell cytoskeletal rearrangements leading to recruitment of lipid microdomains and signalling mediators into the immunological synapse.",
author = "Regina Tavano and Contento, {Rita Lucia} and Baranda, {Sonia Jimenez} and Marzia Soligo and Loretta Tuosto and Santos Manes and Antonella Viola",
year = "2006",
month = "11",
doi = "10.1038/ncb1492",
language = "English",
volume = "8",
pages = "1270--1276",
journal = "Nature Cell Biology",
issn = "1465-7392",
publisher = "Nature Publishing Group",
number = "11",

}

TY - JOUR

T1 - CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse

AU - Tavano, Regina

AU - Contento, Rita Lucia

AU - Baranda, Sonia Jimenez

AU - Soligo, Marzia

AU - Tuosto, Loretta

AU - Manes, Santos

AU - Viola, Antonella

PY - 2006/11

Y1 - 2006/11

N2 - During physiological T-cell stimulation by antigen presenting cells (APCs), a major T-cell membrane rearrangement is known to occur leading to the organization of 'supramolecular activation clusters' at the immunological synapse1,2. A possible role for the synapse is the generation of membrane compartments where signalling may be organized and propagated2. Thus, engagement of the costimulatory molecule CD28 at the immunological synapse promotes the organization of a signalling compartment by inducing cytoskeletal changes and lipid raft accumulation3-5. We identified the actin-binding protein Filamin-A (FLNa) as a novel molecular partner of CD28. We found that, after physiological stimulation, CD28 associated with and recruited FLNa into the immunological synapse, where FLNa organized CD28 signalling. FLNa knockdown by short interfering RNA (siRNA) inhibited CD28-mediated raft accumulation at the immunological synapse and T-cell costimulation. Together, our data indicate that CD28 binding to FLNa is required to induce the T-cell cytoskeletal rearrangements leading to recruitment of lipid microdomains and signalling mediators into the immunological synapse.

AB - During physiological T-cell stimulation by antigen presenting cells (APCs), a major T-cell membrane rearrangement is known to occur leading to the organization of 'supramolecular activation clusters' at the immunological synapse1,2. A possible role for the synapse is the generation of membrane compartments where signalling may be organized and propagated2. Thus, engagement of the costimulatory molecule CD28 at the immunological synapse promotes the organization of a signalling compartment by inducing cytoskeletal changes and lipid raft accumulation3-5. We identified the actin-binding protein Filamin-A (FLNa) as a novel molecular partner of CD28. We found that, after physiological stimulation, CD28 associated with and recruited FLNa into the immunological synapse, where FLNa organized CD28 signalling. FLNa knockdown by short interfering RNA (siRNA) inhibited CD28-mediated raft accumulation at the immunological synapse and T-cell costimulation. Together, our data indicate that CD28 binding to FLNa is required to induce the T-cell cytoskeletal rearrangements leading to recruitment of lipid microdomains and signalling mediators into the immunological synapse.

UR - http://www.scopus.com/inward/record.url?scp=33750533178&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33750533178&partnerID=8YFLogxK

U2 - 10.1038/ncb1492

DO - 10.1038/ncb1492

M3 - Article

C2 - 17060905

AN - SCOPUS:33750533178

VL - 8

SP - 1270

EP - 1276

JO - Nature Cell Biology

JF - Nature Cell Biology

SN - 1465-7392

IS - 11

ER -