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J Biol Chem, Vol. 273, Issue 41, 26281-26284, October 9, 1998
Allows Stable Expression of Receptors
Containing the CD3
Leucine-based Receptor-sorting Motif
From the Institute of Medical Microbiology and Immunology,
University of Copenhagen, The Panum Institute,
DK-2200 Copenhagen, Denmark
The leucine-based motif in the T cell receptor
(TCR) subunit CD3
constitutes a strong internalization signal. In
fully assembled TCR this motif is inactive unless phosphorylated. In
contrast, the motif is constitutively active in CD4/CD3 and
Tac/CD3 chimeras independently of phosphorylation and leads to rapid
internalization and sorting of these chimeras to lysosomal degradation.
Because the TCR
chain rescues incomplete TCR complexes from
lysosomal degradation and allows stable surface expression of fully
assembled TCR, we addressed the question whether TCR has the
potential to mask the CD3 leucine-based motif. By studying
CD4/CD3 and CD16/CD3 chimeras, we found that CD16/CD3 chimeras
associated with TCR. The CD16/CD3-TCR complexes were stably
expressed at the cell surface and had a low spontaneous internalization rate, indicating that the leucine-based motif in these complexes was
inactive. In contrast, the CD4/CD3 chimeras did not associate with
TCR, and the leucine-based motif in these chimeras was
constitutively active resulting in a high spontaneous internalization
rate and low expression of the chimeras at the cell surface. Thus, our data demonstrate that TCR allows stable cell surface expression of
receptors containing CD3 leucine-based motifs by its potential to
mask such motifs.
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