Abstract:
:The current structural model of the B cell antigen receptor (BCR) describes it as a symmetric protein complex in which one membrane-bound immunoglobulin molecule (mIg) is noncovalently bound on each side by an Ig-alpha/Ig-beta heterodimer. Using peptide-tagged Ig-alpha proteins, blue native polyacrylamide gel electrophoresis (BN-PAGE), and biosynthetical labeling of B cells, we find that the mIg:Ig-alpha/Ig-beta complex has a stoichiometry of 1:1 and not 1:2. An anti-Flag stimulation of B cells coexpressing Flag-tagged and wild-type Ig-alpha proteins results in the phosphorylation of both Ig-alpha proteins, suggesting that on the surface of living B cells, several BCR monomers are in contact with each other. A BN-PAGE analysis after limited detergent lysis provides further evidence for an oligomeric BCR structure.
journal_name
Immunityjournal_title
Immunityauthors
Schamel WW,Reth Mdoi
10.1016/s1074-7613(00)00003-0keywords:
subject
Has Abstractpub_date
2000-07-01 00:00:00pages
5-14issue
1eissn
1074-7613issn
1097-4180pii
S1074-7613(00)00003-0journal_volume
13pub_type
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