The Immunological Synapse

Bromley, Shannon K.; Burack, W. Richard; Johnson, Kenneth G.; Somersalo, Kristina; Sims, Tasha N.; Sumen, Cenk; Davis, Mark M.; Shaw, Andréy S.; Allen, Paul M.; Dustin, Michael L.

doi:10.1146/annurev.immunol.19.1.375

Cited by 815 publications

(608 citation statements)

References 114 publications

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“…4). The mapping of the binding site on domain 1 of CD200R together with the complementary data for CD200 itself [13] shows that the CD200/ CD200R interaction also spans this distance providing evidence for areas of close contact between myeloid and other cells in addition to the 'classical' synapse described for T cell interactions [2,11]. Interactions between the membrane proteins of myeloid and cells other than lymphocytes are less well characterized than those of T cells and dendritic cells, but it is notable that the CD47/signal regulatory protein (SIRP) § interaction also spans four IgSF domains although in this case the SIRP § contains three domains and CD47 one domain [20].…”

Section: Discussionmentioning

confidence: 90%

“…In T cells these proteins often interact with other proteins with two IgSF domains in an end-to-end topology. For these interactions to occur, the opposing cell membranes need to come into close proximity and the size of the interacting proteins has been shown to be important in the formation of the immunological synapse and triggering of T cells [10][11][12]. Mutagenesis analysis of CD200 indicated that the N-terminal (membrane-distal) domain of CD200 contains the CD200R binding site [13].…”

Section: Introductionmentioning

confidence: 99%

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The CD200 and CD200 receptor cell surface proteins interact through their N‐terminal immunoglobulin‐like domains

Hatherley

Barclay

2004

Eur J Immunol

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CD200 (OX2) is a broadly distributed cell surface glycoprotein that interacts with a receptor on myeloid cells (CD200R) involved in regulation of macrophage function. Both CD200 and CD200R contain two Ig superfamily domains like many other leukocyte membrane proteins. Site‐directed mutagenesis of CD200R showed that, like CD200, it interacted through its N‐terminal domain. This indicated that the cell‐cell interaction spans four Ig superfamily domains and this distance is similar to many interactions found between T cells and antigen‐presenting cells. This suggests that this topology is also important in interactions of CD200 on a variety of cells with CD200R on myeloid cells, and comparable contact sites may be important mediating regulation in other cell‐cell interactions. The mutagenesis showed that the binding involved the predicted GFCC′ face of its N‐terminal domain, like that of CD200, suggesting that the interaction evolved from a homotypic interaction.

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Section: Discussionmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 99%

The CD200 and CD200 receptor cell surface proteins interact through their N‐terminal immunoglobulin‐like domains

Hatherley

Barclay

2004

Eur J Immunol

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“…Initially, it was thought that these assemblies were large and involved extensive immunoreceptor clustering. For example, it has been suggested that the immunological synapse that forms between the T cell and the Ag-presenting cell facilitates T cell receptor signaling by clustering the receptor and other signaling molecules [20]. Recent studies indicated, however, that initiation of T cell receptor-mediated signaling could occur early and could largely precede the formation of the mature immunological synapse [21,22].…”

Section: Discussionmentioning

confidence: 99%

“…In control cells exposed to 125 I-IgE instead of anti-Fc 4 RI Ab, most of the 125 I-IgEFc 4 RI complexes (94±8%; mean ± SD, n=4) were found in the high-density fractions of the sucrose gradient (fractions [11][12][13][14][15][16][17][18][19][20][21][22], and only a small portion (5.8±2.2%) was found in the low-density fractions (fractions 1-10; Fig. 1E, F).…”

Section: Differences In Degranulation Calcium Response and Drm Recrumentioning

confidence: 99%

Signaling assemblies formed in mast cells activated via Fcϵ receptor I dimers

et al. 2004

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Although aggregation of the Fc 4 receptor I (Fc 4 RI) is necessary for Ag-mediated mast cell triggering, the relationship between the extent of the Fc 4 RI aggregation and subsequent biochemical and topographical events is incompletely understood. In this study, we analyzed the activation events induced by Fc 4 RI dimers, elicited by binding of anti-Fc 4 RI mAb to rat basophilic leukemia cells. We found that, in contrast to extensively aggregated Fc 4 RI, receptor dimers (1) induced a less extensive association of Fc 4 RI with detergent-resistant membranes, (2) delayed the tyrosine phosphorylation and membrane recruitment of several signaling molecules, (3) triggered a slower but more sustained increase in concentration of free cytoplasmic calcium, (4) induced degranulation which was not inhibited at higher concentrations of the cross-linking mAb, and (5) failed to produce clusters of Fc 4 RI, Syk kinase and Grb2 adapter in osmiophilic membranes, as detected by immunogold electron microscopy on membrane sheets. Despite striking differences in the topography of Fc 4 RI dimers and multimers, biochemical differences were less pronounced. The combined data suggest that Fc 4 RI-activated mast cells propagate signals from small signaling domains formed around dimerized/oligomerized Fc 4 RI; formation of large Fc 4 RI aggregates in osmiophilic membranes seems to promote both strong receptor triggering and rapid termination of the signaling responses.

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“…T cell-APC interactions have been studied dynamically in vitro and components of the molecular structures that comprise the synapse have been elegantly characterized [1,2,3]. More recently in vivo documentation of T cell and APC trafficking and interactions have been documented, especially through the use of two photon confocal microscopy [4,5,6,7,8,9].…”

Section: Introductionmentioning

confidence: 99%

T cell–antigen-presenting cell interactions visualized in vivo in a model of antigen-specific inflammation

Rosenbaum

Ronick

Song

et al. 2008

Clinical Immunology

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Videomicroscopy is being used increasingly to characterize the interaction of T cells and antigenpresenting cells (APCs) within lymphatic tissues but has not been reported, to our knowledge, at sites of inflammation. We employed intravital videomicroscopy to study an anterior uveitis model using DO11.10 T cells and ovalbumin (OVA). T cell movement in iris was consistent with a random walk independent of the presence of recognized antigen and had a lateral speed slower than T cells in lymph node. Lingering of T cells adjacent to APCs suggested that they were physically interacting. This apparent contact demonstrated antigen specificity when comparing results from DO11.10 cells with OVA versus bovine serum albumin (BSA) loaded APCs but not when comparing results from OVA-loaded APCs with DO11.10 versus HA clonotype 6.5 T cells. Further studies with this model system should clarify the contribution of T cell-APC communication at a site of inflammation, infection, or immunization.

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The Immunological Synapse

Cited by 815 publications

References 114 publications

The CD200 and CD200 receptor cell surface proteins interact through their N‐terminal immunoglobulin‐like domains

The CD200 and CD200 receptor cell surface proteins interact through their N‐terminal immunoglobulin‐like domains

Signaling assemblies formed in mast cells activated via Fcϵ receptor I dimers

T cell–antigen-presenting cell interactions visualized in vivo in a model of antigen-specific inflammation

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