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1
*
Section of Rheumatology, Departments of Medicine and
Pathology, University of Chicago, Chicago, IL 60637; and
Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742
3 Abbreviations used in this paper: BCR, B cell Ag receptor; AMCA, 7-amino-4-methylcoumarin-3-acetic acid; BLNK, B cell linker protein; GFP, green fluorescent protein; ITAM, immunoreceptor tyrosine-based activation motif; Lamp-1, lysosome-associated membrane protein-1; MIIC, MHC class II-enriched compartment; PDGF, platelet-derived growth factor; PDGFR, platelet-derived growth factor receptor; PLC, phospholipase C; PVDF, polyvinylidene difluoride; SH2, Src homology 2; SNARE, soluble N-ethylmalemide-sensitive factor attachment protein receptor; TfR, transferrin receptor.
Ags that cross-link the B cell Ag receptor are preferentially and
rapidly delivered to the MHC class II-enriched compartment for
processing into peptides and subsequent loading onto MHC class II.
Proper sorting of Ag/receptor complexes requires the recruitment of Syk
to the phosphorylated immunoreceptor tyrosine-based activation motif
tyrosines of the B cell Ag receptor constituent Ig
. We postulated
that the Ig nonimmunoreceptor tyrosine-based activation motif
tyrosines, Y176 and Y204, contributed to
receptor trafficking. Ig(Y
F176,204)/Ig
receptors
were targeted to late endosomes, but were excluded from the vesicle
lumen and could not facilitate the presentation of Ag to T cells.
Subsequent analysis demonstrated that phosphorylation of
Y176/Y204 recruited the B cell linker protein,
Vav, and Grb2. Reconstitution of Ig(YF176,204)/Ig
with the B cell linker protein rescued both receptor-facilitated Ag
presentation and entry into the MHC class II-enriched compartment.
Thus, aggregation accelerates receptor trafficking by recruiting two
separate signaling modules required for transit through sequential
checkpoints.
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