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  The Dok-3/Grb2 adaptor module promotes inducible association of the lipid phosphatase SHIP with the BCR in a coreceptor-independent manner.

Manno, B., Oellerich, T., Schnyder, T., Corso, J., Lösing, M., Neumann, K., et al. (2016). The Dok-3/Grb2 adaptor module promotes inducible association of the lipid phosphatase SHIP with the BCR in a coreceptor-independent manner. European Journal of Immunology, 46(11), 2520-2530. doi:10.1002/eji.201646431.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-3662-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-799A-1
Genre: Journal Article

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 Creators:
Manno, B., Author
Oellerich, T., Author
Schnyder, T., Author
Corso, J.1, Author              
Lösing, M., Author
Neumann, K., Author
Urlaub, H.1, Author              
Batista, F. D., Author
Engelke, M., Author
Wienands, J., Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              

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Free keywords: B cell inhibition; BCR; Dok-3; Grb2; Plasma membrane recruitment; SHIP
 Abstract: The SH2 domain-containing inositol 5'-phosphatase (SHIP) plays a key role in preventing autoimmune phenomena by limiting antigen-mediated B cell activation. SHIP function is thought to require the dual engagement of the BCR and negative regulatory coreceptors as only the latter appear capable of recruiting SHIP from the cytosol to the plasma membrane by virtue of phosphorylated immunoreceptor tyrosine-based inhibitory motifs. Here we demonstrate a coreceptor-independent membrane recruitment and function of SHIP in B cells. In the absence of coreceptor ligation, SHIP translocates to sites of BCR activation through a concerted action of the protein adaptor unit Dok-3/Grb2 and phosphorylated BCR signaling components. Our data reveal auto-inhibitory SHIP activation by the activated BCR and suggest an unexpected negative-regulatory capacity of immunoreceptor tyrosine-based activation motifs in Igα and Igβ.

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Language(s): eng - English
 Dates: 2016-08-232016-11
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/eji.201646431
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Title: European Journal of Immunology
Source Genre: Journal
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Pages: - Volume / Issue: 46 (11) Sequence Number: - Start / End Page: 2520 - 2530 Identifier: -