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The adaptor protein CIN85 assembles intracellular signaling clusters for B cell activation.

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Wong,  L. E.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Schwiegk,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Fünfgeld,  K.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Habeck,  M.
Research Group of Statistical Inverse-Problems in Biophysics, MPI for Biophysical Chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Kühn, J., Wong, L. E., Pirkuliyeva, S., Schulz, K., Schwiegk, C., Fünfgeld, K., et al. (2016). The adaptor protein CIN85 assembles intracellular signaling clusters for B cell activation. Science Signaling, 9(434): ra66. doi:10.1126/scisignal.aad6275.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002A-F551-F
Abstract
The adaptor molecule Cbl-interacting protein of 85 kD (CIN85) regulates signaling from a number of cell surface receptors, such as growth factor receptors and antigen receptors on lymphocytes. Because of its multidomain structure, CIN85 is thought to act as a classical adaptor protein that connects functionally distinct components of a given signaling pathway through diverse protein domains. However, we found that in B lymphocytes, CIN85 functions to oligomerize SLP-65, which is the central effector protein of the B cell receptor (BCR). Therefore, CIN85 trimerizes through a carboxyl-terminal, coiled-coil domain. The multiple Src homology 3 (SH3) domains of trimeric CIN85 molecules associated with multiple SLP-65 molecules, which recruited further CIN85 trimers, thereby perpetuating the oligomerization process. Formation of this oligomeric signaling complex in resting B cells rendered the cells poised for the efficient initiation of intracellular signaling upon BCR stimulation. Our data suggest that the functionality of signaling cascades does not rely solely on the qualitative linkage of their various components but requires a critical number of effectors to become concentrated in signaling complexes.