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

Kläsener, K., Maity, P. C., Hobeika, E., Yang, J., & Reth, M. (2014). B cell activation involves nanoscale receptor reorganizations and inside-out signaling by Syk. eLife, 3, 1-17.

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 Creators:
Kläsener, Kathrin1, Author              
Maity, Palash C.2, Author
Hobeika, Elias1, Author              
Yang, Jianying1, Author              
Reth, Michael1, Author              
Affiliations:
1Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243645              
2Max Planck Society, ou_persistent13              

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 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.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: eDoc: 701186
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Title: eLife
Source Genre: Journal
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Pages: - Volume / Issue: 3 Sequence Number: - Start / End Page: 1 - 17 Identifier: -