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 wellbeing and fitness and illness. the 1st chapters evaluation new insights into the meeting of BCR parts and their association at the mobilephone floor. next contributions concentrate on the molecular interactions that attach the BCR with significant intracellular signaling pathways akin to 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. additionally, a key mechanism of the way B cells take into account their cognate antigen is mentioned intimately. Altogether, the discoveries offered supply a greater figuring out of B mobile biology and aid to give an explanation for a few B cell-mediated pathogenicities, like autoimmune phenomena or the formation of B telephone tumors, whereas additionally paving the way in which for ultimately scuffling with those diseases.
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Proc Natl Acad Sci USA 99(20):13014–13019 Guloglu FB, Roman CA (2006) Precursor B cell receptor signaling activity can be uncoupled from surface expression. J Immunol 176(11):6862–6872 Guo B, Kato RM, Garcia-Lloret M, Wahl MI, Rawlings DJ (2000) Engagement of the human pre-B cell receptor generates a lipid raft-dependent calcium signaling complex. Immunity 13 (2):243–253 Hardy RR, Hayakawa K (2001) B cell development pathways. Annu Rev Immunol 19:595–621 Herzog S, Jumaa H (2012) Self-recognition and clonal selection: autoreactivity drives the generation of B cells.
The Assembly of the BCR Monomer and the Formation of BCR Oligomers It is well accepted now that BCR monomer is a 1:1 complex of mIg molecule and Igα/Igβ heterodimer. What is less clear is how exactly it is assembled, especially the relative orientation of Igα or Igβ toward the mIg molecule. On the one hand, a study of the assembly and intracellular transport of the BCR suggested that the Igβ is closer to the mHC than Igα (Brouns et al. 1995). On the other hand, the conservation of polar amino acids in the Igα TM region, and the finding that only the Receptor Dissociation and B-Cell Activation 37 glycosylation of Igα but not that of Igβ varies upon binding to different mIg isotypes, favored the notion that Igα is closer to the mHC than Igβ (Campbell et al.
In fact, it was shown that simply disrupting the cytoskeleton with drugs such as Latrunculin A (Lat-A) can induce strong signaling, depending on the BCR signaling components (Mattila et al. 2013; Treanor et al. 2010). In our recent Fab-PLA study, treating B cells with Lat-A also resulted in the loss of Fab-PLA signals for BCR:BCR proximity. However, whether the dissociation of the oligomeric BCR following antigen binding is caused by the disruption of actin cytoskeleton remains to be determined.