Pirkuliyeva, Sona

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Wong, Leo E."],["dc.contributor.author","Bhatt, Arshiya"],["dc.contributor.author","Erdmann, Philipp S."],["dc.contributor.author","Hou, Zhen"],["dc.contributor.author","Maier, Joachim"],["dc.contributor.author","Pirkuliyeva, Sona"],["dc.contributor.author","Engelke, Michael"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Plitzko, Jürgen"],["dc.contributor.author","Wienands, Jürgen"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2020-12-10T18:09:53Z"],["dc.date.available","2020-12-10T18:09:53Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41467-020-14544-1"],["dc.identifier.eissn","2041-1723"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73787"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Tripartite phase separation of two signal effectors with vesicles priming B cell responsiveness"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","ra66"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","434"],["dc.bibliographiccitation.journal","Science Signaling"],["dc.bibliographiccitation.lastpage","15"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Kühn, Julius"],["dc.contributor.author","Wong, Leo E."],["dc.contributor.author","Pirkuliyeva, Sona"],["dc.contributor.author","Schulz, Kathrin"],["dc.contributor.author","Schwiegk, Claudia"],["dc.contributor.author","Fünfgeld, Kevser Gencalp"],["dc.contributor.author","Keppler, Selina"],["dc.contributor.author","Batista, Facundo D."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Habeck, Michael"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Wienands, Jürgen"],["dc.date.accessioned","2017-09-07T11:44:50Z"],["dc.date.available","2017-09-07T11:44:50Z"],["dc.date.issued","2016"],["dc.description.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."],["dc.identifier.doi","10.1126/scisignal.aad6275"],["dc.identifier.gro","3141661"],["dc.identifier.isi","000378944100004"],["dc.identifier.pmid","27353366"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6564"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [SFB 860, TRR 130]; Max Planck Society"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1937-9145"],["dc.relation.issn","1945-0877"],["dc.title","The adaptor protein CIN85 assembles intracellular signaling clusters for B cell activation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","ra79"],["dc.bibliographiccitation.issue","339"],["dc.bibliographiccitation.journal","Science Signaling"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Engelke, Michael"],["dc.contributor.author","Pirkuliyeva, Sona"],["dc.contributor.author","Kuehn, Julius"],["dc.contributor.author","Wong, Leo E."],["dc.contributor.author","Boyken, Janina"],["dc.contributor.author","Herrmann, Nadine"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Wienands, Jürgen"],["dc.date.accessioned","2017-09-07T11:45:36Z"],["dc.date.available","2017-09-07T11:45:36Z"],["dc.date.issued","2014"],["dc.description.abstract","The traditional view of how intracellular effector proteins are recruited to the B cell antigen receptor (BCR) complex at the plasma membrane is based on the occurrence of direct protein-protein interactions, as exemplified by the recruitment of the tyrosine kinase Syk (spleen tyrosine kinase) to phosphorylated motifs in BCR signaling subunits. By contrast, the subcellular targeting of the cytosolic adaptor protein SLP-65 (Src homology 2 domain-containing leukocyte adaptor protein of 65 kD), which serves as a proximal Syk substrate, is unclear. We showed that SLP-65 activation required its association at vesicular compartments in resting B cells. A module of similar to 50 amino acid residues located at the amino terminus of SLP-65 anchored SLP-65 to the vesicles. Nuclear magnetic resonance spectroscopy showed that the SLP-65 amino terminus was structurally disordered in solution, but could bind in a structured manner to noncharged lipid components of cellular membranes. Our finding that preformed vesicular signaling scaffolds are required for B cell activation indicates that vesicles may deliver preassembled signaling cargo to sites of BCR activation."],["dc.identifier.doi","10.1126/scitranslmed.2005104"],["dc.identifier.gro","3142070"],["dc.identifier.isi","000341192700003"],["dc.identifier.pmid","25140054"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4211"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Assoc Advancement Science"],["dc.relation.eissn","1937-9145"],["dc.relation.issn","1945-0877"],["dc.title","Macromolecular assembly of the adaptor SLP-65 at intracellular vesicles in resting B cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]