Abstract:
:Recent studies point to glycolipid-enriched membrane (GEM) microdomains as the critical sites for TCR-mediated signal transduction. However, whether the TCR complex is localized in the GEM domain is not well-defined. In the present study, we analyzed localization of the TCR-CD3 complex in the GEM domain by isolating the GEM fraction with sucrose density gradient centrifugation. Although 10% of TCRzeta chains was localized in the GEM fraction, most of the TCR complexes were excluded from the GEM before and after T cell activation, and the amount of TCRzeta in the GEM was not increased after activation. However, the tyrosine-phosphorylated form of TCRzeta was strongly concentrated in the GEM fraction upon TCR engagement. A kinetic study revealed that tyrosine phosphorylation of TCRzeta occurred initially in the Triton X-100-soluble membrane fraction followed by the accumulation of phosphorylated TCRzeta in the GEM. Thus, these results indicate that phosphorylated TCRzeta migrates into the GEM domains on T cell activation. We speculate that the GEM microdomains may function as a reservoir of activation signals from triggered TCR.
journal_name
Int Immunoljournal_title
International immunologyauthors
Kosugi A,Saitoh S,Noda S,Yasuda K,Hayashi F,Ogata M,Hamaoka Tdoi
10.1093/intimm/11.9.1395subject
Has Abstractpub_date
1999-09-01 00:00:00pages
1395-401issue
9eissn
0953-8178issn
1460-2377journal_volume
11pub_type
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