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Laboratoire d’Immunologie Cellulaire, Institut National de la Santé et de la Recherche Médicale, Unité 543, Groupe Hospitalier Pitié-Salpêtrière, Paris, France; and
Laboratoire d’Immunopharmacologie Moléculaire, Centre National de la Recherche Scientifique, Unité Propre de Recherche 415, Institut Cochin de Génétique Moléculaire, Paris, France
CD5 is a cell surface receptor that negatively regulates B cell
function, but whose relationship to the immunoreceptor tyrosine-based
inhibitory motif (ITIM) family of B cell inhibitory receptors is
unclear. Using Fc
type IIB receptor-CD5 chimeras encompassing the
cytoplasmic domain of CD5, we previously showed that a particular
region of the molecule containing two tyrosine residues, Y429 and Y441,
in an amino acid stretch similar to the Src autophosphorylation motif
and a putative ITIM, respectively, antagonized early signaling events
triggered through the B cell receptor (BCR). In this study, we provide
evidences that only Y429 is mandatory for the inhibition by CD5 of the
calcium response activated via the BCR. This residue also efficiently
controls inhibition of the Ras/extracellular signal-related kinase-2
pathway. Analyzing the membrane translocation of the AKT
protooncogene using its 3'-phosphoinositide-specific pleckstrin
homology domain fused to the green fluorescent protein as a probe, we
also show that CD5 strongly impairs its cellular redistribution and
demonstrate the role played by Y429 in this process. We finally report
that Y429 controls almost exclusively CD5 phosphorylation as well as
inhibition of BCR-triggered IL-2 production upon coaggregation of the
two receptors. Thus, CD5 uses an ITIM-independent strategy, centered on
Y429, the major tyrosine-phosphorylated residue in its cytoplasmic
domain, to inhibit BCR activation.
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