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  Tripartite phase separation of two signal effectors with vesicles priming B cell responsiveness.

Wong, L. E., Bhatt, A., Erdmann, P. S., Hou, Z., Maier, J., Pirkuliyeva, S., et al. (2020). Tripartite phase separation of two signal effectors with vesicles priming B cell responsiveness. Nature Communications, 11: 848. doi:10.1038/s41467-020-14544-1.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-A94E-6 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-A952-0
Genre: Journal Article

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 Creators:
Wong, L. E.1, Author              
Bhatt, A., Author
Erdmann, P. S., Author
Hou, Z., Author
Maier, J.1, Author              
Pirkuliyeva, S., Author
Engelke, M., Author
Becker, S.1, Author              
Plitzko, J., Author
Wienands, J., Author
Griesinger, C.1, Author              
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 Abstract: Antibody-mediated immune responses rely on antigen recognition by the B cell antigen receptor (BCR) and the proper engagement of its intracellular signal effector proteins. Src homology (SH) 2 domain-containing leukocyte protein of 65 kDa (SLP65) is the key scaffold protein mediating BCR signaling. In resting B cells, SLP65 colocalizes with Cbl-interacting protein of 85 kDa (CIN85) in cytoplasmic granules whose formation is not fully understood. Here we show that effective B cell activation requires tripartite phase separation of SLP65, CIN85, and lipid vesicles into droplets via vesicle binding of SLP65 and promiscuous interactions between nine SH3 domains of the trimeric CIN85 and the proline-rich motifs (PRMs) of SLP65. Vesicles are clustered and the dynamical structure of SLP65 persists in the droplet phase in vitro. Our results demonstrate that phase separation driven by concerted transient interactions between scaffold proteins and vesicles is a cellular mechanism to concentrate and organize signal transducers.

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Language(s): eng - English
 Dates: 2020-02-12
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41467-020-14544-1
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Title: Nature Communications
Source Genre: Journal
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Pages: 9 Volume / Issue: 11 Sequence Number: 848 Start / End Page: - Identifier: -