Urlaub, Henning

[["dc.bibliographiccitation.firstpage","893"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Cellular Signalling"],["dc.bibliographiccitation.lastpage","900"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Neumann, Konstantin"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Heine, Ines"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Engelke, Michael"],["dc.date.accessioned","2018-11-07T08:56:49Z"],["dc.date.available","2018-11-07T08:56:49Z"],["dc.date.issued","2011"],["dc.description.abstract","B cells require signals transduced by the B cell antigen receptor (BCR) to provide humoral adaptive immunity. These signals are modulated by co-receptors like the Fc gamma receptor IIb (Fc gamma RIIb) that prevents activation of B cells after co-ligation with the BCR. Positive and negative effectors need to be precisely organized into signaling complexes, which requires adapter proteins like the growth factor receptor-bound protein 2 (Grb2). Here, we address the question how Grb2-mediated signal integration is affected by Fc gamma RIIb. Our data reveal that concomitant engagement of BCR and Fc gamma RIIb leads to markedly increased Grb2-mediated formation of ternary protein complexes comprising downstream of kinase-3 (Dok-3), Grb2, and the SH2 domain-containing inositol phosphatase (SHIP). Consistently, we found Grb2 to be required for full Fc gamma RIIb-mediated negative regulation. To investigate how Fc gamma RIIb influences the entire Grb2 interactions, we utilized quantitative mass spectrometry to make a differential interactome analysis. This approach revealed a shift of Grb2 interactions towards negative regulators like Dok-3. SHIP and SHP-2 and reduced binding to other proteins like CD19. Hence, we provide evidence that Grb2-mediated signal integration is a dynamic process that is important for the crosstalk between the BCR and its co-receptor Fc gamma RIIb. (C) 2011 Elsevier Inc. All rights reserved."],["dc.description.sponsorship","DFG research group [FOR 521]"],["dc.identifier.doi","10.1016/j.cellsig.2011.01.015"],["dc.identifier.isi","000288977400017"],["dc.identifier.pmid","21262349"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23243"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.relation.issn","0898-6568"],["dc.title","Fc gamma receptor IIb modulates the molecular Grb2 interaction network in activated B cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2520"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","European Journal of Immunology"],["dc.bibliographiccitation.lastpage","2530"],["dc.bibliographiccitation.volume","46"],["dc.contributor.author","Manno, Birgit"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Schnyder, Tim"],["dc.contributor.author","Corso, Jasmin"],["dc.contributor.author","Loesing, Marion"],["dc.contributor.author","Neumann, Konstantin"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Batista, Facundo D."],["dc.contributor.author","Engelke, Michael"],["dc.contributor.author","Wienands, Juergen"],["dc.date.accessioned","2018-11-07T10:05:58Z"],["dc.date.available","2018-11-07T10:05:58Z"],["dc.date.issued","2016"],["dc.description.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 the 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 Ig alpha and Ig beta."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [TRR130]; University Medicine Gottingen"],["dc.identifier.doi","10.1002/eji.201646431"],["dc.identifier.isi","000392940100006"],["dc.identifier.pmid","27550373"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39006"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1521-4141"],["dc.relation.issn","0014-2980"],["dc.title","The Dok-3/Grb2 adaptor module promotes inducible association of the lipid phosphatase SHIP with the BCR in a coreceptor-independent manner"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]