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dc.contributor.authorHeinzelmann, Katharina
dc.contributor.authorScholz, Barbara A
dc.contributor.authorNowak, Agnes
dc.contributor.authorFossum, Even
dc.contributor.authorKremmer, Elisabeth
dc.contributor.authorHaas, Juergen
dc.contributor.authorFrank, Ronald
dc.contributor.authorKempkes, Bettina
dc.date.accessioned2017-02-02T14:21:56Z
dc.date.available2017-02-02T14:21:56Z
dc.date.issued2010-12
dc.identifier.citationKaposi's sarcoma-associated herpesvirus viral interferon regulatory factor 4 (vIRF4/K10) is a novel interaction partner of CSL/CBF1, the major downstream effector of Notch signaling. 2010, 84 (23):12255-64 J. Virol.en
dc.identifier.issn1098-5514
dc.identifier.pmid20861242
dc.identifier.doi10.1128/JVI.01484-10
dc.identifier.urihttp://hdl.handle.net/10033/620801
dc.description.abstractIn cells infected with the Kaposi's sarcoma-associated herpesvirus (KSHV), CSL/CBF1 signaling is essential for viral replication and promotes the survival of KSHV-infected cells. CSL/CBF1 is a DNA adaptor molecule which recruits coactivator and corepressor complexes to regulate viral and cellular gene transcription and which is a major downstream effector molecule of activated Notch. The interaction of KSHV RTA and LANA with CSL/CBF1 has been shown to balance the lytic and latent viral life cycle. Here we report that a third KSHV protein, viral interferon regulatory factor 4 (vIRF4/K10), but none of the three other KSHV-encoded vIRFs, interacts with CSL/CBF1. Two regions of vIRF4 with dissimilar affinities contribute to CSL/CBF1 binding. Similar to Notch, vIRF4 targets the hydrophobic pocket in the beta trefoil domain of CSL/CBF1 through a short peptide motif which closely resembles a motif found in Notch but does not strictly follow the ΦWΦP consensus conserved in human and mouse Notch proteins. Our results suggest that vIRF4 might compete with Notch for CSL/CBF1 binding and signaling.
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshBinding, Competitiveen
dc.subject.meshCell Line, Tumoren
dc.subject.meshChromatography, Affinityen
dc.subject.meshDNA Primersen
dc.subject.meshElectrophoresis, Polyacrylamide Gelen
dc.subject.meshElectrophoretic Mobility Shift Assayen
dc.subject.meshHerpesvirus 8, Humanen
dc.subject.meshHumansen
dc.subject.meshImmunoblottingen
dc.subject.meshImmunoglobulin J Recombination Signal Sequence-Binding Proteinen
dc.subject.meshImmunoprecipitationen
dc.subject.meshInterferon Regulatory Factorsen
dc.subject.meshPlasmidsen
dc.subject.meshProtein Bindingen
dc.subject.meshReceptors, Notchen
dc.subject.meshSignal Transductionen
dc.subject.meshTwo-Hybrid System Techniquesen
dc.subject.meshViral Proteinsen
dc.titleKaposi's sarcoma-associated herpesvirus viral interferon regulatory factor 4 (vIRF4/K10) is a novel interaction partner of CSL/CBF1, the major downstream effector of Notch signaling.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for infection research. Inhoffenstr. 7. 38124 Braunschweig, Germany.en
dc.identifier.journalJournal of virologyen
refterms.dateFOA2018-06-12T21:40:04Z
html.description.abstractIn cells infected with the Kaposi's sarcoma-associated herpesvirus (KSHV), CSL/CBF1 signaling is essential for viral replication and promotes the survival of KSHV-infected cells. CSL/CBF1 is a DNA adaptor molecule which recruits coactivator and corepressor complexes to regulate viral and cellular gene transcription and which is a major downstream effector molecule of activated Notch. The interaction of KSHV RTA and LANA with CSL/CBF1 has been shown to balance the lytic and latent viral life cycle. Here we report that a third KSHV protein, viral interferon regulatory factor 4 (vIRF4/K10), but none of the three other KSHV-encoded vIRFs, interacts with CSL/CBF1. Two regions of vIRF4 with dissimilar affinities contribute to CSL/CBF1 binding. Similar to Notch, vIRF4 targets the hydrophobic pocket in the beta trefoil domain of CSL/CBF1 through a short peptide motif which closely resembles a motif found in Notch but does not strictly follow the ΦWΦP consensus conserved in human and mouse Notch proteins. Our results suggest that vIRF4 might compete with Notch for CSL/CBF1 binding and signaling.


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