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B cell antigen receptors of the IgM and IgD classes are clustered in different protein islands that are altered during B cell activation

MPG-Autoren

Maity,  Palash Chandra
BIOSS Centre for Biological Signaling Studies, University of Freiburg;
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Jumaa,  H.
Institute of Immunology, Ulm University;
Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Reth,  Michael
BIOSS Centre for Biological Signaling Studies, University of Freiburg;
Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Zitation

Maity, P. C., Blount, A., Jumaa, H., Ronneberger, O., Lillemeier, B. F., & Reth, M. (2015). B cell antigen receptors of the IgM and IgD classes are clustered in different protein islands that are altered during B cell activation. Science Signaling, 8, ra93. doi:10.1126/scisignal.2005887.


Zitierlink: https://hdl.handle.net/someHandle/test/escidoc:902528
Zusammenfassung
The B cell antigen receptors (BCRs) play an important role in the clonal selection of B cells and their differentiation into antibody-secreting plasma cells. Mature B cells have both immunoglobulin M (IgM) and IgD types of BCRs, which have identical antigen-binding sites and are both associated with the signaling subunits Igα and Igβ, but differ in their membrane-bound heavy chain isoforms. By two-color direct stochastic optical reconstruction microscopy (dSTORM), we showed that IgM-BCRs and IgD-BCRs reside in the plasma membrane in different protein islands with average sizes of 150 and 240 nm, respectively. Upon B cell activation, the BCR protein islands became smaller and more dispersed such that the IgM-BCRs and IgD-BCRs were found in close proximity to each other. Moreover, specific stimulation of one class of BCR had minimal effects on the organization of the other. These conclusions were supported by the findings from two-marker transmission electron microscopy and proximity ligation assays. Together, these data provide evidence for a preformed multimeric organization of BCRs on the plasma membrane that is remodeled after B cell activation.