Endosomal targeting by the cytoplasmic tail of membrane immunoglobulin.
Membrane-bound immunoglobulin (mIg) of the IgG, IgA, and IgE classes have conserved cytoplasmic tails. To investigate the function of these tails, a B cell line was transfected with truncated or mutated gamma2a heavy chains. Transport to the endosomal compartment of antigen bound by the B cell antigen receptor did not occur in the absence of the cytoplasmic tail; and one or two mutations, respectively, in the Tyr-X-X-Met motif of the tail partially or completely interrupted the process. Experiments with chimeric antigen receptors confirmed these findings. Thus, a role for the cytoplasmic tail of mIg heavy chains in endosomal targeting of antigen is revealed.
Weiser
P
P
Max-Planck-Institut für Immunbiologie, Stübeweg 51, D-79108 Freiburg, Germany.
Müller
R
R
Braun
U
U
Reth
M
M
D000818:Animals; D017951:Antigen Presentation; D001402:B-Lymphocytes / Q000276:immunology*; D001692:Biological Transport; D003593:Cytoplasm; D019281:Dimerization; D011992:Endosomes / Q000276:immunology*; D007142:Immunoglobulin gamma-Chains / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007156:Immunologic Memory; D051379:Mice; D009154:Mutation; D011947:Receptors, Antigen, B-Cell / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D014162:Transfection; D014407:Tumor Cells, Cultured
D007142:Immunoglobulin gamma-Chains; D011947:Receptors, Antigen, B-Cell; D011993:Recombinant Fusion Proteins