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Mediates B Cell Receptor Constitutive Internalization1
*
CJF 9501 and
Unité 255, INSERM and
UMR 144 CNRS, Molecular Mechanisms of Intracellular Trafficking Laboratory, Institut Curie, Paris;
§
Laboratoire d’Histocompatibilité, Centre Régional de Transfusion Sanguine and
¶
INSERM Unité 74, Institut de Virologie, Faculté de Médecine, Strasbourg; and
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Centre d’Immunologie INSERM-CNRS de Marseille-Luminy, Marseille, France
B lymphocytes express Ag receptors (BCR) that are composed
of ligand binding subunits, the membrane Igs, associated with Ig 
/Ig
ß heterodimers. One main BCR function is to bind and to internalize
Ags. Peptides generated from these internalized Ags may be presented to
T lymphocytes. Here, we have analyzed the involvement of BCR Ig /Ig
ß components in BCR constitutive endocytosis. The role of Ig
subunit in BCR constitutive endocytosis was first determined in the
context of an IgM-based BCR. In contrast with BCR that contain
wild-type Ig , surface BCR lacking Ig cytoplasmic domain were
not constitutively internalized. The respective roles of Ig and Ig
ß subunits were then analyzed by expressing chimeric molecules
containing the cytoplasmic domains of either subunits in a B cell line.
Only the Ig cytoplasmic domain contained an internalization signal
that allowed constitutive endocytosis of Ig chimeras via coated
pits and accumulation in sorting-recycling endosomes. This
internalization signal is contained in its immunoreceptor
tyrosine-based activation motif. These results indicate that Ig ,
through its immunoreceptor tyrosine-based activation motif, may account
for the ability of IgM/IgD BCR to constitutively internalize monovalent
Ags.
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