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B cell activation involves nanoscale receptor reorganizations and inside-out signaling by Syk

By K. Kläsener, P. Maity, E. Hobeika, J. Yang and M. Reth

Abstract

Binding of antigen to the B cell antigen receptor (BCR) initiates a multitude of events resulting in B cell activation. How the BCR becomes signaling-competent upon antigen binding is still a matter of controversy. Using a high-resolution proximity ligation assay (PLA) to monitor the conformation of the BCR and its interactions with co-receptors at a 10-20 nm resolution, we provide direct evidence for the opening of BCR dimers during B cell activation. We also show that upon binding Syk opens the receptor by an inside-out signaling mechanism that amplifies BCR signaling. Furthermore, we found that on resting B cells, the coreceptor CD19 is in close proximity with the IgD-BCR and on activated B cells with the IgM-BCR, indicating nanoscale reorganization of receptor clusters during B cell activation

Year: 2014
OAI identifier: oai:escidoc.org:escidoc:2348808
Provided by: MPG.PuRe
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