2015
Complement membrane attack complexes activate noncanonical NF-κB by forming an Akt+NIK+ signalosome on Rab5+ endosomes
Jane-wit D, Surovtseva YV, Qin L, Li G, Liu R, Clark P, Manes TD, Wang C, Kashgarian M, Kirkiles-Smith NC, Tellides G, Pober JS. Complement membrane attack complexes activate noncanonical NF-κB by forming an Akt+NIK+ signalosome on Rab5+ endosomes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 9686-9691. PMID: 26195760, PMCID: PMC4534258, DOI: 10.1073/pnas.1503535112.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBaculoviral IAP Repeat-Containing 3 ProteinClathrinComplement Membrane Attack ComplexCoronary VesselsEndocytosisEndosomesEnzyme StabilityFlow CytometryHuman Umbilical Vein Endothelial CellsHumansHydrazonesInhibitor of Apoptosis ProteinsMice, SCIDNF-kappa BProtein BiosynthesisProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktrab5 GTP-Binding ProteinsRNA, Small InterferingSecretory VesiclesSignal TransductionTNF Receptor-Associated Factor 3Ubiquitin-Protein LigasesConceptsNF-κB-inducing kinaseMembrane attack complexNoncanonical NF-κBGenome-wide siRNA screenComplement membrane attack complexNIK stabilizationDynamin-dependent mannerNoncanonical NF-κB signalingEndothelial cellsActive Rab5Attack complexSiRNA screenNF-κBAkt activationCytokine-mediated activationNF-κB signalingIκB kinaseSignalosomeRab5EndosomesKinaseAktInternalizationCoronary endothelial cellsActivation
2011
Mitoxosome: a mitochondrial platform for cross‐talk between cellular stress and antiviral signaling
Tal MC, Iwasaki A. Mitoxosome: a mitochondrial platform for cross‐talk between cellular stress and antiviral signaling. Immunological Reviews 2011, 243: 215-234. PMID: 21884179, PMCID: PMC3170140, DOI: 10.1111/j.1600-065x.2011.01038.x.Peer-Reviewed Original ResearchConceptsCellular stressMitochondrial functionCell biologic analysesViral recognitionInnate immune signalingDynamic relocalizationAntiviral signalingImmune signalingMitochondriaAntiviral responseMultiple pathwaysAntiviral immunityCurrent understandingRecent findingsSignalingViral replicationInnate responseIntegrated viewBiologic analysisRecent studiesSignalosomeRelocalizationKey componentStressIntegral platform
2009
COP9 Signalosome Interacts ATP-dependently with p97/Valosin-containing Protein (VCP) and Controls the Ubiquitination Status of Proteins Bound to p97/VCP*
Cayli S, Klug J, Chapiro J, Fröhlich S, Krasteva G, Orel L, Meinhardt A. COP9 Signalosome Interacts ATP-dependently with p97/Valosin-containing Protein (VCP) and Controls the Ubiquitination Status of Proteins Bound to p97/VCP*. Journal Of Biological Chemistry 2009, 284: 34944-34953. PMID: 19826004, PMCID: PMC2787357, DOI: 10.1074/jbc.m109.037952.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAdenosine TriphosphateAmino Acid SequenceAnimalsCell Cycle ProteinsCOP9 Signalosome ComplexHumansMiceMolecular Sequence DataMultiprotein ComplexesNIH 3T3 CellsPeptide HydrolasesProtein BindingProtein SubunitsRecombinant Fusion ProteinsUbiquitinationValosin Containing ProteinConceptsP97/valosin-containing proteinValosin-containing proteinUbiquitin/proteasome systemCOP9 signalosomeUbiquitination statusUbiquitinated proteinsProteasome degrades ubiquitinated proteinsATP-dependent mannerProteasome regulatory particleATP-dependent complexesUbiquitin E3 ligasesOligoubiquitin chainsCSN complexE3 ligasesPolyubiquitinated substratesRegulatory particleIsopeptidase activityProteasome systemDeubiquitinase USP15Subunit 5ProteinSignalosomeDegradation pathwayCSN5Key mediator
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