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Characterization of the Kaposi's sarcoma-associated herpesvirus K1 signalosome

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dc.contributor.authorLee, Bok-Soo-
dc.contributor.authorLee, Sun-Hwa-
dc.contributor.authorFeng, Pinghui-
dc.contributor.authorChang, Heesoon-
dc.contributor.authorCho, Nam-Hyuk-
dc.contributor.authorJung, Jae U.-
dc.date.accessioned2010-01-12T02:32:32Z-
dc.date.available2010-01-12T02:32:32Z-
dc.date.issued2005-09-15-
dc.identifier.citationJ Virol. 2005 Oct;79(19):12173-84.en
dc.identifier.issn0022-538X (Print)-
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16160144-
dc.identifier.urihttp://hdl.handle.net/10371/29617-
dc.description.abstractKaposi's sarcoma (KS) is a multifocal angiogenic tumor and appears to be a hyperplastic disorder caused, in part, by local production of inflammatory cytokines. The K1 lymphocyte receptor-like protein of KS-associated herpesvirus (KSHV) efficiently transduces extracellular signals to elicit cellular activation events through its cytoplasmic immunoreceptor tyrosine-based activation motif (ITAM). To further delineate K1-mediated signal transduction, we purified K1 signaling complexes and identified its cellular components. Upon stimulation, the K1 ITAM was efficiently tyrosine phosphorylated and subsequently interacted with cellular Src homology 2 (SH2)-containing signaling proteins Lyn, Syk, p85, PLCgamma2, RasGAP, Vav, SH2 domain-containing protein tyrosine phosphatase 1/2, and Grab2 through its phosphorylated tyrosine residues. Mutational analysis demonstrated that each tyrosine residue of K1 ITAM contributed to the interactions with cellular signaling proteins in distinctive ways. Consequently, these interactions led to the marked augmentation of cellular signal transduction activity, evidenced by the increase of cellular tyrosine phosphorylation and intracellular calcium mobilization, the activation of NF-AT and AP-1 transcription factor activities, and the production of inflammatory cytokines. These results demonstrate that KSHV K1 effectively recruits a set of cellular SH2-containing signaling molecules to form the K1 signalosome, which elicits downstream signal transduction and induces inflammatory cytokine production.en
dc.language.isoen-
dc.publisherAmerican Society for Microbiologyen
dc.subjectAmino Acid Motifsen
dc.subjectCalcium/analysisen
dc.subjectCell Cycle Proteins/metabolismen
dc.subjectCell Lineen
dc.subjectCytokines/analysisen
dc.subjectCytoplasm/chemistryen
dc.subjectDNA Mutational Analysisen
dc.subjectDNA-Binding Proteins/metabolismen
dc.subjectEnzyme Precursors/metabolismen
dc.subjectHerpesvirus 8, Human/*physiologyen
dc.subjectHumansen
dc.subjectIntracellular Signaling Peptides and Proteinsen
dc.subjectNFATC Transcription Factorsen
dc.subjectNuclear Proteins/metabolismen
dc.subjectPhospholipase C gammaen
dc.subjectPhosphorylationen
dc.subjectProtein Bindingen
dc.subjectProtein Phosphatase 1en
dc.subjectProtein Tyrosine Phosphatases/metabolismen
dc.subjectProtein-Tyrosine Kinases/metabolismen
dc.subjectProto-Oncogene Proteins/metabolismen
dc.subjectProto-Oncogene Proteins c-vaven
dc.subject*Signal Transductionen
dc.subjectTranscription Factor AP-1/metabolismen
dc.subjectTranscription Factors/metabolismen
dc.subjectType C Phospholipases/metabolismen
dc.subjectTyrosine/metabolismen
dc.subjectViral Proteins/genetics/metabolism/*physiologyen
dc.subjectsrc-Family Kinases/metabolismen
dc.titleCharacterization of the Kaposi's sarcoma-associated herpesvirus K1 signalosomeen
dc.typeArticleen
dc.contributor.AlternativeAuthor이복수-
dc.contributor.AlternativeAuthor이선화-
dc.contributor.AlternativeAuthor장희순-
dc.contributor.AlternativeAuthor조남혁-
dc.contributor.AlternativeAuthor정재유-
dc.identifier.doi10.1128/JVI.79.19.12173-12184.2005-
Appears in Collections:
College of Medicine/School of Medicine (의과대학/대학원)Microbiology (미생물학전공)Journal Papers (저널논문_미생물학전공)
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