The role of glycosyl phosphatidyl inositol (GPI)-anchored cell surface proteins in T-cell activation

Loertscher, Rolf; Lavery, Paula

doi:10.1016/s0966-3274(02)00013-8

Cited by 53 publications

(39 citation statements)

References 26 publications

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“…Although CD48 is a GPI-anchored receptor and lacks intracytoplasmic domains, it can be physically associated to G proteins or to the SRC family of tyrosine kinases in glycolipid-enriched microdomains of the cell membrane (41,42). This may be mediated by Lck, which is phosphorylated upon CD48 cross-linking (43)(44)(45). Interestingly, lck Ϫ/Ϫ CD8 ϩ T cells expressed higher levels of CD48 when compared with wt T cells (our unpublished data).…”

Section: Discussionmentioning

confidence: 78%

NK Cells Stimulate Proliferation of T and NK Cells through 2B4/CD48 Interactions

Assarsson

Kambayashi

Schatzle

et al. 2004

The Journal of Immunology

103

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Few studies have addressed the consequences of physical interactions between NK and T cells, as well as physical interactions among NK cells themselves. We show in this study that NK cells can enhance T cell activation and proliferation in response to CD3 cross-linking and specific Ag through interactions between 2B4 (CD244) on NK cells and CD48 on T cells. Furthermore, 2B4/CD48 interactions between NK cells also enhanced proliferation of NK cells in response to IL-2. Overall, these results suggest that NK cells augment the proliferation of neighboring T and NK cells through direct cell-cell contact. These results provide new insights into NK cell-mediated control of innate and adaptive immunity and demonstrate that receptor/ligand-specific cross talk between lymphocytes may occur in settings other than T-B cell or T-T cell interactions.

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Section: Discussionmentioning

confidence: 78%

NK Cells Stimulate Proliferation of T and NK Cells through 2B4/CD48 Interactions

Assarsson

Kambayashi

Schatzle

et al. 2004

The Journal of Immunology

103

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“…This conclusion has since been challenged by various findings (14, 16, 44 -46), whereas other results suggest that raft reorganization indeed plays a key role in physiological T-cell activation (13,47,48). Part of the initial evidence suggesting involvement of rafts in T-cell signaling was provided by observations that antibody-induced cross-linking of GPI-proteins or GM1-bound CTB can trigger intracellular signaling events resembling some of the early events occurring during physiological T-cell activation (8,17,19,49,50). It has been suggested that cross-linking of these molecules on the lymphocyte surface triggers intracellular signaling events by causing lateral redistribution and/or growth of rafts within the plasma membrane, favoring the enrichment of proteins promoting cell activation, and the depletion of species that antagonize such activation (e.g.…”

Section: Discussionmentioning

confidence: 99%

Artificially Lipid-anchored Proteins Can Elicit Clustering-induced Intracellular Signaling Events in Jurkat T-Lymphocytes Independent of Lipid Raft Association

Wang¹,

Leventis

Silvius

2005

Journal of Biological Chemistry

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We have incorporated artificial lipid-anchored streptavidin conjugates with fully saturated or polyunsaturated lipid anchors into the plasma membranes of Jurkat T-lymphocytes to assess previous conclusions that the activation of signaling processes induced in these cells by clustering of endogenous glycosylphosphatidylinositol-anchored proteins or ganglioside GM1 depends specifically on the association of these membrane components with lipid rafts. Lipid-anchored streptavidin conjugates could be incorporated into Jurkat or other mammalian cell surfaces by inserting biotinylated phosphatidylethanolamine-polyethyleneglycols (PE-PEGs) and subsequently binding streptavidin to the cell-incorporated PE-PEGs. Saturated dipalmitoyl-PE-PEG-streptavidin conjugates prepared in this manner partitioned substantially into the detergent-insoluble membrane fraction isolated from Jurkat or fibroblast cells, whereas polyunsaturated dilinoleoyl-PE-PEG-anchored conjugates were wholly excluded from this fraction, consistent with the differences in the affinities of the two types of lipid anchors for liquidordered membrane domains. Remarkably, however, antibody-mediated cross-linking of either dipalmitoylor dilinoleoyl-PE-PEG-anchored streptavidin conjugates in Jurkat cells induced elevation of cytoplasmic calcium levels and tyrosine phosphorylation of the scaffolding protein linker of T-cell activation in a manner similar to that observed upon cross-linking of endogenous CD59 or ganglioside GM1. The amplitude of the cross-linking-stimulated elevation of cytoplasmic calcium moreover showed an essentially identical dependence on the level of incorporated streptavidin conjugate for either type of lipid anchor. Confocal fluorescence microscopy revealed that PE-PEG-streptavidin conjugates with saturated versus polyunsaturated anchors showed very similar surface distributions vis à vis GM1 or CD59 under conditions where one or both species were cross-linked. These results indicate that crosslinking of diverse proteins anchored only to the outer leaflet of the plasma membrane can induce activation of Jurkat T-cell-signaling responses, but they appear to contradict previous suggestions that this phenomenon rests specifically on the association of such species with lipid rafts.

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“…Others and we have shown that cross-linking of GPI-anchored proteins on T cells, such as CD90, Ly-6, CD48, and CD59 results in phosphorylation of protein tyrosine kinases like Lck (10,11). Thus, GPI-anchored proteins have potential to provide costimulatory signals during T cell activation.…”

mentioning

confidence: 88%

Sequential Cooperation of CD2 and CD48 in the Buildup of the Early TCR Signalosome

Muhammad

Schiller

Förster

et al. 2009

The Journal of Immunology

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The buildup of TCR signaling microclusters containing adaptor proteins and kinases is prerequisite for T cell activation. One hallmark in this process is association of the TCR with lipid raft microdomains enriched in GPI-proteins that have potential to act as accessory molecules for TCR signaling. In this study, we show that GPI-anchored CD48 but not CD59 was recruited to the immobilized TCR/CD3 complex upon activation of T cells. CD48 reorganization was vital for T cell IL-2 production by mediating lateral association of the early signaling component linker for activated T cells (LAT) to the TCR/CD3 complex. Furthermore, we identified CD2 as an adaptor linking the Src protein tyrosine kinase Lck and the CD48/LAT complex to TCR/CD3: CD2 associated with TCR/CD3 upon T cell activation irrespective of CD48 expression, while association of CD48 and LAT with the TCR/CD3 complex depended on CD2. Consequently, our data indicate that CD2 and CD48 cooperate hierarchically in the buildup of the early TCR signalosome; CD2 functions as the master switch recruiting CD48 and Lck. CD48 in turn shuttles the transmembrane adapter molecule LAT.

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The role of glycosyl phosphatidyl inositol (GPI)-anchored cell surface proteins in T-cell activation

Cited by 53 publications

References 26 publications

NK Cells Stimulate Proliferation of T and NK Cells through 2B4/CD48 Interactions

NK Cells Stimulate Proliferation of T and NK Cells through 2B4/CD48 Interactions

Artificially Lipid-anchored Proteins Can Elicit Clustering-induced Intracellular Signaling Events in Jurkat T-Lymphocytes Independent of Lipid Raft Association

Sequential Cooperation of CD2 and CD48 in the Buildup of the Early TCR Signalosome

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