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Aggregation of Lipid Rafts Accompanies Signaling via the T Cell Antigen Receptor
Open accessAbstract
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.
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Metadata
- Authors
- Janes, P. W., Ley, S. C., & Magee, A. I.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 1999-10-18
- Volume
- 147
- Issue
- 2
- Pages
- 447-461
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W1988530230
- Cited by
- 796
- References
- 1
- FWCI
- 22.51
- Type
- journal article
- Language
- en
- Open access
- green
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