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Review
. 2003 Dec;110(4):401-10.
doi: 10.1111/j.1365-2567.2003.01770.x.

Models of signal transduction through the B-cell antigen receptor

Roland Geisberger  1 , Reto Crameri, Gernot Achatz
Affiliations
Review

Models of signal transduction through the B-cell antigen receptor

Roland Geisberger et al. Immunology. 2003 Dec.
No abstract available

PubMed Disclaimer

Figures

Figure 1
Figure 1
Amino acid alignment of the C-terminal domains of mouse mIg-isotypes. Light shading, domains as predicted by the Kyte and Doolittle algorithm; medium shading, domains as predicted by PHDtopology; dark shading, domains as predicted by the Klein algorithm. In the case of mIgA, the transmembrane and cytoplasmic domains are encoded by just one exon. Concerning the extracellular domain, light and dark shade are coherent.
Figure 2
Figure 2
Model of the BCR complex. The mIg backbone, comprising two immunoglobulin heavy chains, two immunoglobulin light chains, the transmembrane region and the cytoplasmic domain, is associated with the two coat proteins Igα and Igβ. Both sheath proteins, inside their intracellular tail harbour an ITAM motif. On antigen contact, the tyrosines of the ITAMs are phosphorylated by members of the Src-family kinsases.
Figure 3
Figure 3
Model for the initial phosphorylation of the ITAMs within the Igα/Igβ sheath. In principle, two models for the initiation of BCR signalling are discussed: the allosteric activation of cytoplasmic protein–tyrosine kinases upon antigen binding (a), and the activation of cytoplasmic protein–tyrosine kinases upon clustering of two or more BCRs on the membrane (b). However, the kinases leading to the initial phosphorylation event could be preassociated to the cytoplasmic tails of Igα/Igβ (Pre-association model), or the BCRs, as a result of the clustering, are translocated to specialized membrane locations (signalling domain or lipid raft model).
See this image and copyright information in PMC

References

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