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Subunit of the TCR Contains Endocytosis Signals1
*
Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Cientificas-Universidad Autónoma, Madrid, Spain; and
Unité de Biologie des Interactions Cellulaires, Institut Pasteur, Paris, France
Ligand binding to TCR induces its internalization and cell surface
down-modulation. These phenomena contribute to the extinction of
activation signals. Due to the multicomponent nature of the TCR-CD3
complex, its internalization may be mediated by one or several of its
subunits. Although it has been reported that CD3
and CD3
contain
endocytosis motifs involved in the internalization of the TCR-CD3
complex, other subunits could also be involved in this process. For
instance, CD3
and CD
display amino acid sequences reminiscent of
internalization motifs. To investigate whether CD3 bears endocytosis
signals, we have analyzed the internalization capacity of a panel of
deletion and point mutants of CD3 that were expressed on the cell
surface independently of other TCR-CD3 subunits. Here we report that
CD3 displays endocytosis determinants. These data indicate that
CD3 could contribute to the internalization and cell surface
down-regulation of TCR-CD3 complexes. Moreover, the existence of
endocytosis signals in this polypeptide could serve to retrieve
unassembled CD3 subunits or partial CD3 complexes from the plasma
membrane, thus restricting the expression on the cell surface to fully
functional TCR-CD3 complexes.
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