By Tomohiro Kurosaki, Jürgen Wienands
This quantity information our present realizing of the structure and signaling functions of the B mobilephone antigen receptor (BCR) in overall healthiness and sickness. the 1st chapters overview new insights into the meeting of BCR elements and their association at the phone floor. next contributions concentrate on the molecular interactions that attach the BCR with significant intracellular signaling pathways resembling Ca2+ mobilization, membrane phospholipid metabolism, nuclear translocation of NF-kB or the activation of Bruton’s Tyrosine Kinase and MAP kinases. those parts orchestrate cytoplasmic and nuclear responses in addition to cytoskeleton dynamics for antigen internalization. moreover, a key mechanism of ways B cells have in mind their cognate antigen is mentioned intimately. Altogether, the discoveries offered supply a greater knowing of B telephone biology and support to provide an explanation for a few B cell-mediated pathogenicities, like autoimmune phenomena or the formation of B phone tumors, whereas additionally paving the best way for finally struggling with those diseases.
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Extra resources for B Cell Receptor Signaling
1991). We have shown that both IgM-BCR and IgD-BCR are able to form oligomers and both are opened upon activation (Kläsener et al. 2014; Yang and Reth 2010a). However, it is not clear whether they form oligomers separately or together. Earlier studies with B cells expressing both isotypes of BCR showed that stimulation with one type of anti-HC antibodies induces phosphorylation of only the Igα associated with the corresponding BCR (Gold et al. 1991; Schamel and Reth 2000). This suggests that IgM-BCR and IgD-BCR may be physically separated from each other.
Based on these ﬁndings, we proposed that most BCR complexes form auto-inhibited oligomers in resting B cells. Inside the BCR oligomer, the ITAMs of the Igα/Igβ may be orientated in a way that they are not directly available for the phosphorylation mediated by kinases such as Lyn and Syk. Upon antigen binding, BCR oligomers could open, exposing the ITAM of Igα/Igβ tail and 34 J. Yang and M. Reth initiating intracellular signaling. Thus, B-cell activation seems to involve the dissociation of BCR oligomers rather than the cross-linking of BCR monomers as suggested by CLM.
Mutation of a 30 J. Yang and M. Reth tyrosine and a serine residue on this side of the µm HC prevents proper BCR assembly (Sanchez et al. 1993; Shaw et al. 1990). Formerly, it was thought that, similar to the T-cell antigen receptor (TCR), the BCR is a symmetric complex with each of the two mHCs of the mIg molecule bound to one Igα/Igβ heterodimer (Reth 1992). However, this 1:2 stoichiometry was not conﬁrmed by blue native polyacrylamide gel electrophoresis (BN–PAGE), which, together with other biochemical experiments, clearly showed a 1:1 stoichiometry of the mIg:Igα/Igβ complex (Schamel and Reth 2000).