The B cell antigen receptor (BCR) comprises the membrane-bound immunoglobul
in (mIg) molecule and the Ig-alpha/Ig-beta heterodimer. By comparing the st
ability of the IgD-BCR and IgM-BCR in different detergent lysates, we find
that the IgD-BCR is more stable than the IgM-BCR. Analysis of chimeric mIgD
molecules suggests that the delta m transmembrane region is responsible fo
r the more stable association of mIgD with the Ig-alpha/Ig-beta heterodimer
. Further, the differential glycosylation of Ig-alpha molecules, in the two
different BCR complexes, is determined solely by the ectodomains of the mi
g molecules. The implications of these findings for the intracellular trans
port and the signalling capacity of the BCRs are discussed. (C) 2000 Elsevi
er Science Ltd. All rights reserved.