2002
Signaling disrupts mSin3A binding to the Mad1‐like Sin3‐interacting domain of TIEG2, an Sp1‐like repressor
Ellenrieder V, Zhang J, Kaczynski J, Urrutia R. Signaling disrupts mSin3A binding to the Mad1‐like Sin3‐interacting domain of TIEG2, an Sp1‐like repressor. The EMBO Journal 2002, 21: 2451-2460. PMID: 12006497, PMCID: PMC126002, DOI: 10.1093/emboj/21.10.2451.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsBinding SitesCell Cycle ProteinsCHO CellsConsensus SequenceCricetinaeGenes, ReporterKruppel-Like Transcription FactorsMicePhosphorylationProtein BindingRecombinant ProteinsRepressor ProteinsSignal TransductionSin3 Histone Deacetylase and Corepressor ComplexSp1 Transcription FactorTranscription FactorsTransfectionZinc FingersConceptsSin3 interaction domainTranscriptional repressionAnti-proliferative functionMad proteinsRepressor proteinRepression activitySerine/threonine sitesTranscription factorsConstitutive mannerSignaling pathwayRepressionGrowth suppressionFunctional impactTIEG2ProteinRepressorSerine/threonineTIEGTranscriptionPhosphorylationDomainSignalPathwayInteractionBinding
2001
A Conserved α-Helical Motif Mediates the Interaction of Sp1-Like Transcriptional Repressors with the Corepressor mSin3A
Zhang J, Moncrieffe M, Kaczynski J, Ellenrieder V, Prendergast F, Urrutia R. A Conserved α-Helical Motif Mediates the Interaction of Sp1-Like Transcriptional Repressors with the Corepressor mSin3A. Molecular And Cellular Biology 2001, 21: 5041-5049. PMID: 11438660, PMCID: PMC87230, DOI: 10.1128/mcb.21.15.5041-5049.2001.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsApoptosis Regulatory ProteinsBlotting, WesternCell Cycle ProteinsCell DivisionCHO CellsCircular DichroismCricetinaeGenetic VectorsGlutathione TransferaseLuciferasesMolecular Sequence DataMutationPeptide BiosynthesisPlasmidsPrecipitin TestsProtein BindingProtein BiosynthesisProtein Structure, TertiaryRecombinant Fusion ProteinsRepressor ProteinsSequence Homology, Amino AcidSin3 Histone Deacetylase and Corepressor ComplexSp1 Transcription FactorTranscription, GeneticTransforming Growth Factor betaZinc FingersConceptsSp1-like proteinsRepress transcriptionDeacetylase complexRepression motifTranscriptional repressionSin3 histone deacetylase complexBind GC-rich sequencesMechanism of transcriptional repressionSp1-like transcription factorsMSin3A-histone deacetylase complexGC-rich sequencesMammalian cell homeostasisCorepressor mSin3ARepression domainTranscriptional repressorA-helicesMSin3ATranscription factorsTIEG2Antiproliferative functionCell homeostasisMotifTranscriptionRepressionProteinThe activity of the TGFβ-inducible transcription factor TIEG2 is antagonized by the proliferative EGFR-MEK-ERK signaling pathway
Ellenrieder V, Zhang J, Kaczynski J, Urrutia R. The activity of the TGFβ-inducible transcription factor TIEG2 is antagonized by the proliferative EGFR-MEK-ERK signaling pathway. Gastroenterology 2001, 120: a497. DOI: 10.1016/s0016-5085(08)82467-5.Peer-Reviewed Original ResearchThe activity of the TGFβ-inducible transcription factor TIEG2 is antagonized by the proliferative EGFR-MEK-ERK signaling pathway
ELLENRIEDER V, ZHANG J, KACZYNSKI J, URRUTIA R. The activity of the TGFβ-inducible transcription factor TIEG2 is antagonized by the proliferative EGFR-MEK-ERK signaling pathway. Gastroenterology 2001, 120: a497-a497. DOI: 10.1016/s0016-5085(01)82467-7.Peer-Reviewed Original Research
2000
Detailed domain structure and MAP kinase-mediated phosphorylation of the growth suppressor transcription factor, TIEG2
Ellenrieder V, Kaczynski J, Hedin K, Urrutia R. Detailed domain structure and MAP kinase-mediated phosphorylation of the growth suppressor transcription factor, TIEG2. Gastroenterology 2000, 118: a639. DOI: 10.1016/s0016-5085(00)84693-4.Peer-Reviewed Original Research