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B and T lymphocyte attenuator interacts with CD3 ζ and inhibits tyrosine phosphorylation of TCR ζ complex during T‐cell activation
Author(s) -
Wu TingHe,
Zhen Yu,
Zeng Chun,
Yi HuanFa,
Zhao Yong
Publication year - 2007
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1038/sj.icb.7100087
Subject(s) - btla , t cell receptor , lipid raft , immunological synapse , microbiology and biotechnology , t cell , cd3 , tyrosine phosphorylation , phosphorylation , cd28 , biology , signal transduction , jurkat cells , chemistry , antigen , cd8 , immune system , immunology
B and T lymphocyte attenuator (BTLA) is an important negative regulator of T‐cell activation. T‐cell activation involves partitioning of receptors into discrete membrane compartments known as lipid rafts and the formation of an immunological synapse (IS) between the T cell and antigen‐presenting cell (APC). Here we show that after T‐cell stimulation, BTLA co‐clusters with the CD3 ζ and is then involved in IS, as determined by a two‐photon microscope. BTLA can interact with the phosphorylated form of T‐cell receptor (TCR) within the lipid raft, which is associated with the T‐cell signaling complex. Coligation of BTLA with the TCR significantly decreased the amount of phosphorylated TCR‐related signal accumulation in the lipid raft during T‐cell activation. These results suggest that BTLA functions to regulate T‐cell signaling by controlling the phosphorylated form of TCR ζ accumulation in the lipid raft.