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Endosomal Targeting by the Cytoplasmic Tail of Membrane Immunoglobulin

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Science  18 Apr 1997:
Vol. 276, Issue 5311, pp. 407-409
DOI: 10.1126/science.276.5311.407

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Abstract

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 γ2a 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.

  • * These authors contributed equally to this work.

  • Present address: Institut Curie, 12 rue Lhomond, 75005 Paris, France.

  • To whom correspondence should be addressed. E-mail: reth{at}immunbio.mpg.de

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