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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(1): 848. doi:10.1038/s41467-020-14544-1.

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 Creators:
Wong, Leo E.1, Author
Bhatt, Arshiya1, Author
Erdmann, Philipp S.2, Author              
Hou, Zhen2, Author              
Maier, Joachim1, Author
Pirkuliyeva, Sona1, Author
Engelke, Michael1, Author
Becker, Stefan1, Author
Plitzko, Jürgen2, Author              
Wienands, Juergen1, Author
Griesinger, Christian1, Author
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: MEMBRANE CURVATURE; ANTIGEN RECEPTOR; LIQUID-PHASE; BLNK; PROTEIN; SYK; LYMPHOCYTES; GRANULES; DOMAIN; SLP65
 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. Antibody-mediated immune responses rely on antigen recognition by the B cell antigen receptor (BCR) and SLP65 is a key scaffold protein mediating BCR signaling. Here authors show that effective B cell activation requires tripartite phase separation of SLP65, CIN85, and lipid vesicles.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Project name : SFB860 project B05
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Funding organization : Deutsche Forschungsgemeinschaft

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 11 (1) Sequence Number: 848 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723