B Cell Receptor Signaling (Current Topics in Microbiology by Tomohiro Kurosaki, Jürgen Wienands

By Tomohiro Kurosaki, Jürgen Wienands

This quantity information our present knowing of the structure and signaling features of the B mobile antigen receptor (BCR) in healthiness and sickness. the 1st chapters evaluate new insights into the meeting of BCR elements and their association at the cellphone floor. next contributions concentrate on the molecular interactions that attach the BCR with significant intracellular signaling pathways corresponding 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. moreover, a key mechanism of the way B cells take note their cognate antigen is mentioned intimately. Altogether, the discoveries awarded offer a greater knowing of B cellphone biology and support to give an explanation for a few B cell-mediated pathogenicities, like autoimmune phenomena or the formation of B mobile tumors, whereas additionally paving the best way for ultimately scuffling with those diseases.

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References .................................................................................................................................. 28 28 30 30 31 32 32 40 1 Introduction The humoral immune response depends on the activation and clonal expansion of B cells and their differentiation into antibody-producing plasma cells. A B-cell recognizes a specific antigen via its B-cell antigen receptors (BCR), comprising the membrane-bound form of the immunoglobulin (mIg) and the Igα/Igβ heterodimer, the former acting as the antigen binding subunit and the latter as the signaling subunit.

Immunity 32:187–199 Venkitaraman AR, Williams GT, Dariavach P, Neuberger MS (1991) The B-cell antigen receptor of the five immunoglobulin classes. Nature 352:777–781 Vogel SS, Thaler C, Koushik SV (2006) Fanciful FRET. Sci STKE 2006, re2 Wienands J, Reth M (1992) Glycosyl-phosphatidylinositol linkage as a mechanism for cell-surface expression of immunoglobulin D. Nature 356:246–248 Wilson BS, Pfeiffer JR, Surviladze Z, Gaudet EA, Oliver JM (2001) High resolution mapping of mast cell membranes reveals primary and secondary domains of Fc(epsilon)RI and LAT.

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).

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