Membrane-bound immunoglobulin (mlg) of the IgG, IgA, and IgE classes h
ave conserved cytoplasmic tails. To investigate the function of these
tails, a B cell line was transfected with truncated or mutated gamma 2
a heavy chains. Transport to the endosomal compartment of antigen boun
d by the B cell antigen receptor did not occur in the absence of the c
ytoplasmic tail; and one or two mutations, respectively, in the Tyr-X-
X-Met motif of the tail partially or completely interrupted the proces
s. Experiments with chimeric antigen receptors confirmed these finding
s. Thus, a role for the cytoplasmic tail of mlg heavy chains in endoso
mal targeting of antigen is revealed.