scholarly journals Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering

2003 ◽  
Vol 369 (2) ◽  
pp. 301-309 ◽  
Author(s):  
Luca BINI ◽  
Sonia PACINI ◽  
Sabrina LIBERATORI ◽  
Silvia VALENSIN ◽  
Michela PELLEGRINI ◽  
...  
Keyword(s):  
T Cell ◽  
Lipid Rafts ◽  
Antigen Receptor ◽  
Temporal Analysis ◽  
Membrane Microdomains ◽  
T Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Dynamic Structures ◽  
Tcr Signalling

Signalling by immunoreceptors is orchestrated at specific plasma membrane microdomains, referred to as lipid rafts. Here we present a proteomics approach to the temporal analysis of protein association with lipid rafts following T-cell antigen receptor (TCR) triggering. We show that TCR engagement promotes the temporally regulated recruitment of proteins participating in the TCR signalling cascade to lipid rafts. Furthermore, TCR triggering results in profound modifications in the composition of lipid rafts involving a number of proteins associated either directly or indirectly with both plasma and intracellular membranes. Raft-associated proteins can be clustered according to their temporal profile of raft association. The data identify lipid rafts as highly dynamic structures and reveal a dramatic impact of surface TCR triggering not only on components of the TCR signalling machinery but also on proteins implicated in a number of diverse cellular processes.

The role of lipid rafts in T cell antigen receptor (TCR) signalling

2000 ◽  
Vol 12 (1) ◽  
pp. 23-34 ◽  
Author(s):  
Peter W. Janes ◽  
Steven C. Ley ◽  
Anthony I. Magee ◽  
Panagiotis S. Kabouridis
Keyword(s):  
T Cell ◽  
Lipid Rafts ◽  
Antigen Receptor ◽  
T Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Tcr Signalling

T cell antigen receptor (TCR) transmembrane peptides colocalize with TCR, not lipid rafts, in surface membranes

2002 ◽  
Vol 215 (1) ◽  
pp. 12-19 ◽  
Author(s):  
Xin M. Wang ◽  
Julianne T. Djordjevic ◽  
Veronica Bender ◽  
Nicholas Manolios
Keyword(s):  
T Cell ◽  
Lipid Rafts ◽  
Antigen Receptor ◽  
T Cell Antigen Receptor ◽  
Transmembrane Peptides ◽  
Cell Antigen Receptor ◽  
Cell Antigen

scholarly journals Aggregation of Lipid Rafts Accompanies Signaling via the T Cell Antigen Receptor

1999 ◽  
Vol 147 (2) ◽  
pp. 447-461 ◽  
Author(s):  
Peter W. Janes ◽  
Steven C. Ley ◽  
Anthony I. Magee
Keyword(s):  
T Cell ◽  
Tyrosine Phosphorylation ◽  
Lipid Rafts ◽  
Antigen Receptor ◽  
Cross Linking ◽  
Tcr Signaling ◽  
T Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Associated Proteins

The role of lipid rafts in T cell antigen receptor (TCR) signaling was investigated using fluorescence microscopy. Lipid rafts labeled with cholera toxin B subunit (CT-B) and cross-linked into patches displayed characteristics of rafts isolated biochemically, including detergent resistance and colocalization with raft-associated proteins. LCK, LAT, and the TCR all colocalized with lipid patches, although TCR association was sensitive to nonionic detergent. Aggregation of the TCR by anti-CD3 mAb cross-linking also caused coaggregation of raft-associated proteins. However, the protein tyrosine phosphatase CD45 did not colocalize to either CT-B or CD3 patches. Cross-linking of either CD3 or CT-B strongly induced tyrosine phosphorylation and recruitment of a ZAP-70(SH2)2–green fluorescent protein (GFP) fusion protein to the lipid patches. Also, CT-B patching induced signaling events analagous to TCR stimulation, with the same dependence on expression of key TCR signaling molecules. Targeting of LCK to rafts was necessary for these events, as a nonraft- associated transmembrane LCK chimera, which did not colocalize with TCR patches, could not reconstitute CT-B–induced signaling. Thus, our results indicate a mechanism whereby TCR engagement promotes aggregation of lipid rafts, which facilitates colocalization of LCK, LAT, and the TCR whilst excluding CD45, thereby triggering protein tyrosine phosphorylation.

scholarly journals Regulation of T-cell antigen receptor signalling by Syk tyrosine protein kinase.

1997 ◽  
Vol 17 (8) ◽  
pp. 4434-4441 ◽  
Author(s):  
S Latour ◽  
M Fournel ◽  
A Veillette
Keyword(s):  
T Cells ◽  
T Cell ◽  
Tyrosine Phosphorylation ◽  
Antigen Receptor ◽  
Gammadelta T Cells ◽  
T Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Tcr Signalling

T-cell antigen receptor (TCR) signalling has been shown to involve two classes of tyrosine protein kinases: the Src-related kinases p56(lck) and p59(fyr), and the Zap-70/Syk family kinases. Lck and FynT are postulated to initiate TCR-triggered signal transduction by phosphorylating the CD3 and zeta subunits of the TCR complex. This modification permits the recruitment of Zap-70 and Syk, which are presumed to amplify the TCR-triggered signal, by phosphorylating additional intracellular proteins. While Zap-70 is expressed in all T cells, Syk is present in thymocytes and mature T-cell populations such as intraepithelial gammadelta T cells and naive alphabeta T cells. To better understand the role of Syk in these cells, its impact on the physiology of an antigen-specific T-cell line was tested. Our results showed that compared to Zap-70 alone, Syk was a strong positive regulator of antigen receptor-induced signals in BI-141 cells. Surprisingly, they indicated that, like Src family kinases, Syk augmented TCR-triggered tyrosine phosphorylation of CD3/zeta. Syk, but not Zap-70 alone, could also stimulate tyrosine phosphorylation of a zeta-bearing chimera in transiently transfected Cos-1 cells. Finally, evidence was provided that Syk has the capacity to directly phosphorylate a zeta-derived peptide in vitro. These findings suggested that Syk may have a unique role in T cells, as a consequence of its ability to efficiently phosphorylate multiple components of the TCR signalling cascade. Furthermore, they raised the possibility that Syk can regulate the initiation of TCR signalling, by promoting phosphorylation of the immunoreceptor tyrosine-based activation motifs of the TCR complex.

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