Urlaub, Henning

[["dc.bibliographiccitation.firstpage","135"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Immunological Reviews"],["dc.bibliographiccitation.lastpage","149"],["dc.bibliographiccitation.volume","232"],["dc.contributor.author","Neumann, Konstantin"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Wienands, Jürgen"],["dc.date.accessioned","2011-04-21T09:31:50Z"],["dc.date.accessioned","2021-10-27T13:22:42Z"],["dc.date.available","2011-04-21T09:31:50Z"],["dc.date.available","2021-10-27T13:22:42Z"],["dc.date.issued","2009"],["dc.description.abstract","The growth factor receptor-bound protein 2 (Grb2) is a ubiquitously expressed and evolutionary conserved adapter protein possessing a plethora of described interaction partners for the regulation of signal transduction. In B lymphocytes, the Grb2-mediated scaffolding function controls the assembly and subcellular targeting of activating as well as inhibitory signalosomes in response to ligation of the antigen receptor. Also, integration of simultaneous signals from B-cell coreceptors that amplify or attenuate antigen receptor signal output relies on Grb2. Hence, Grb2 is an essential signal integrator. The key question remains, however, of how pathway specificity can be maintained during signal homeostasis critically required for the balance between immune cell activation and tolerance induction. Here, we summarize the molecular network of Grb2 in B cells and introduce a proteomic approach to elucidate the interactome of Grb2 in vivo."],["dc.identifier.doi","10.1111/j.1600-065X.2009.00845.x"],["dc.identifier.isi","000271057600011"],["dc.identifier.pmid","19909361"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6258"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92119"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1600-065X"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.subject.mesh","Animals"],["dc.subject.mesh","B-Lymphocytes"],["dc.subject.mesh","GRB2 Adaptor Protein"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Immune Tolerance"],["dc.subject.mesh","Lymphocyte Activation"],["dc.subject.mesh","Protein Interaction Domains and Motifs"],["dc.subject.mesh","Protein Multimerization"],["dc.subject.mesh","Proteomics"],["dc.subject.mesh","Receptor Cross-Talk"],["dc.subject.mesh","Receptors, Antigen, B-Cell"],["dc.subject.mesh","Signal Transduction"],["dc.title","The B-lymphoid Grb2 interaction code."],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e7541"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","PLoS One"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Galli, Soledad"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Hitt, Reiner"],["dc.contributor.author","Hesse, Doerte"],["dc.contributor.author","Opitz, Lennart"],["dc.contributor.author","Plessmann, Uwe"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Poderoso, Juan Jose"],["dc.contributor.author","Jares-Erijman, Elizabeth A."],["dc.contributor.author","Jovin, Thomas M."],["dc.date.accessioned","2019-07-09T11:52:42Z"],["dc.date.available","2019-07-09T11:52:42Z"],["dc.date.issued","2009"],["dc.description.abstract","Extracellular signal-regulated protein kinase 1 and 2 (ERK1/2) are members of the MAPK family and participate in the transduction of stimuli in cellular responses. Their long-term actions are accomplished by promoting the expression of specific genes whereas faster responses are achieved by direct phosphorylation of downstream effectors located throughout the cell. In this study we determined that hERK1 translocates to the mitochondria of HeLa cells upon a proliferative stimulus. In the mitochondrial environment, hERK1 physically associates with (i) at least 5 mitochondrial proteins with functions related to transport (i.e. VDAC1), signalling, and metabolism; (ii) histones H2A and H4; and (iii) other cytosolic proteins. This work indicates for the first time the presence of diverse ERK-complexes in mitochondria and thus provides a new perspective for assessing the functions of ERK1 in the regulation of cellular signalling and trafficking in HeLa cells."],["dc.format.extent","18"],["dc.identifier.doi","10.1371/journal.pone.0007541"],["dc.identifier.fs","569017"],["dc.identifier.pmid","19847302"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5824"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60253"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Public Library of Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.subject.ddc","610"],["dc.subject.mesh","Amino Acid Sequence"],["dc.subject.mesh","Cell Proliferation"],["dc.subject.mesh","Gene Expression Profiling"],["dc.subject.mesh","Gene Expression Regulation, Enzymologic"],["dc.subject.mesh","Gene Expression Regulation, Neoplastic"],["dc.subject.mesh","Glutathione Transferase"],["dc.subject.mesh","Hela Cells"],["dc.subject.mesh","Humans"],["dc.subject.mesh","MAP Kinase Signaling System"],["dc.subject.mesh","Mitochondria"],["dc.subject.mesh","Mitogen-Activated Protein Kinase 3"],["dc.subject.mesh","Molecular Sequence Data"],["dc.subject.mesh","Proteomics"],["dc.subject.mesh","Sequence Homology, Amino Acid"],["dc.subject.mesh","Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization"],["dc.title","A new paradigm for MAPK: structural interactions of hERK1 with mitochondria in HeLa cells."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]