Stability of the B cell antigen receptor complex.

The B cell antigen receptor (BCR) comprises the membrane-bound immunoglobulin (mIg) molecule and the Ig-alpha/Ig-beta heterodimer. By comparing the stability 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 deltam transmembrane region is responsible for 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 mIg molecules. The implications of these findings for the intracellular transport and the signalling capacity of the BCRs are discussed.