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(Received for publication, February 27, 1996, and in revised form, August 12, 1996)
From the The transmembrane domain of T cell receptor (TCR)
Volume 271, Number 48,
Issue of November 29, 1996
pp. 30417-30425
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
That
Impairs CD3
Association
,
and
Centro de Biología Molecular Severo
Ochoa,
contains a conserved immunoreceptor tyrosine-based activation-like
motif consisting of a duplicated YXXL sequence. The motif
is also present in TCR
, the equivalent chain to TCR in 
T
lymphocytes but is absent in TCR
and TCR. To determine the
putative role of this sequence in TCR·CD3 complex assembly and signal
transduction, a TCR chain cDNA was mutated in the C-terminal
tyrosine of the motif, cloned in an expression vector, and transfected
into TCR-negative Jurkat cells. Transfectants of the mutated chain
(MUT) expressed, on average, much less TCR·CD3 complex on the
membrane than wild type TCR transfectants. Radiolabeling experiments
suggested that the mutation caused a loose association of the CD3
chain resulting in a defective assembly. However, stimulation of high
TCR·CD3 expressing wild type and MUT clones with monoclonal
antibodies and Staphylococcus aureus enterotoxin B resulted
in similar levels of CD25 and CD69 expression, interleukin-2 secretion,
and TCR·CD3 complex down-regulation. By contrast, MUT cells were
clearly resistant to activation-induced cell death, and they did not
express CD95-ligand upon activation. These results suggest a
differentiated intracellular signaling pathway leading to apoptosis in
which Tyr-TM11 of the immunoreceptor tyrosine-based activation
motif-like motif and CD3 appear to be involved.
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