2025
G3BP1 ribonucleoprotein complexes regulate focal adhesion protein mobility and cell migration
Boraas L, Hu M, Martino P, Thornton L, Vejnar C, Zhen G, Zeng L, Parker D, Cox A, Giraldez A, Su X, Mayr C, Wang S, Nicoli S. G3BP1 ribonucleoprotein complexes regulate focal adhesion protein mobility and cell migration. Cell Reports 2025, 44: 115237. PMID: 39883578, PMCID: PMC11923778, DOI: 10.1016/j.celrep.2025.115237.Peer-Reviewed Original ResearchConceptsRNA-binding proteinsFocal adhesionsCell migrationStress granulesRNA-dependent mannerProtein mobilityFA proteinsRNA bindingDimerization domainSubcellular localizationRibonucleoprotein complexNon-stress conditionsFA sizeCell speedG3BP1RibonucleoproteinFA localizationBiological processesB-actinMRNAProteinCellsFA functionMigrationLocalization
2023
Split aminoacyl-tRNA synthetases for proximity-induced stop codon suppression
Jiang H, Ambrose N, Chung C, Wang Y, Söll D, Tharp J. Split aminoacyl-tRNA synthetases for proximity-induced stop codon suppression. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2219758120. PMID: 36787361, PMCID: PMC9974479, DOI: 10.1073/pnas.2219758120.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetasesCodon suppressionStop codon suppressionGene expressionOrthogonal aminoacyl-tRNA synthetasesRelevant protein-protein interactionsSynthetic biology toolsSmall molecule rapamycinControl gene expressionProtein-protein interactionsLevel of transcriptionAbscisic acidDimerization domainMammalian cellsBiology toolsGene translationTranslational levelMolecular switchStop codonHuman cellsMolecular inputsUseful biotechnologySynthetasesExpressionTherapeutic applications
2010
Crystal Structure of CCM3, a Cerebral Cavernous Malformation Protein Critical for Vascular Integrity*
Li X, Zhang R, Zhang H, He Y, Ji W, Min W, Boggon TJ. Crystal Structure of CCM3, a Cerebral Cavernous Malformation Protein Critical for Vascular Integrity*. Journal Of Biological Chemistry 2010, 285: 24099-24107. PMID: 20489202, PMCID: PMC2911348, DOI: 10.1074/jbc.m110.128470.Peer-Reviewed Original ResearchMeSH KeywordsApoptosis Regulatory ProteinsBinding, CompetitiveBrainCrystallography, X-RayDimerizationHemangioma, Cavernous, Central Nervous SystemHumansKineticsMembrane ProteinsMolecular ConformationMutationPaxillinProtein ConformationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProto-Oncogene ProteinsConceptsN-terminal dimerization domainPaxillin LD motifsCerebral cavernous malformationsAlpha-helical proteinsLD motifsCCM complexHomology domainFocal adhesionsDimerization domainMolecular basisHydrophobic pocketHuman populationCCM3 mutationsMutationsCCM3Crystal structureVascular integrityCCM2DomainPaxillinProteinMotifCCM1InteractionCells
2005
The Requirement for Mechanical Coupling Between Head and S2 Domains in Smooth Muscle Myosin ATPase Regulation and its Implications for Dimeric Motor Function
Tama F, Feig M, Liu J, Brooks C, Taylor K. The Requirement for Mechanical Coupling Between Head and S2 Domains in Smooth Muscle Myosin ATPase Regulation and its Implications for Dimeric Motor Function. Journal Of Molecular Biology 2005, 345: 837-854. PMID: 15588830, DOI: 10.1016/j.jmb.2004.10.084.Peer-Reviewed Original ResearchConceptsMyosin headsAlpha-helicesATP-dependent molecular motorSmooth muscle myosin IIMyosin II regulationCoiled-coil domainMuscle myosin IIInhibited stateMolecular motorsMyosin IIATPase regulationDimerization domainElastic network normal mode analysisAlpha-helixDomain movementsHomology modelingFunction of molecular motorsMyosinBiochemical dataConformational transitionRegulationNormal mode analysisExperimental structural dataStructural dataHeptad
2001
Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein
Mattoon D, Gupta K, Doyon J, Loll P, DiMaio D. Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein. Oncogene 2001, 20: 3824-3834. PMID: 11439346, DOI: 10.1038/sj.onc.1204523.Peer-Reviewed Original ResearchConceptsBovine papillomavirus E5 proteinE5 proteinDimer interfacePlatelet-derived growth factor β receptorEssential glutamine residueHeterologous dimerization domainGrowth factor β receptorNon-productive interactionsReceptor tyrosine phosphorylationFocus formation assayPDGF β-receptorDimerization domainHomodimeric proteinTyrosine phosphorylationGenetic methodsGlutamine residuesActive chimerasΒ receptorActive orientationFormation assaysProtein helicesProteinPosition 17ReceptorsPhosphorylation
1997
Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation
Burke C, Lemmon M, Coren B, Engelman D, Stern D. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene 1997, 14: 687-696. PMID: 9038376, DOI: 10.1038/sj.onc.1200873.Peer-Reviewed Original ResearchConceptsReceptor tyrosine kinasesTransmembrane domainEpidermal growth factor receptorSignal transductionWild-type domainSecond-site mutationsPosition 664Dimerization domainGrowth factor receptorTyrosine kinaseGlycophorin AFactor receptorValine substitutionDimerizationMutationsTransductionGlutamic acidDomainWeak dimerizationMutantsKinaseSignalingProteinEGFChimeras
1996
A Zinc-binding Domain Involved in the Dimerization of RAG1
Rodgers K, Bu Z, Fleming K, Schatz D, Engelman D, Coleman J. A Zinc-binding Domain Involved in the Dimerization of RAG1. Journal Of Molecular Biology 1996, 260: 70-84. PMID: 8676393, DOI: 10.1006/jmbi.1996.0382.Peer-Reviewed Original ResearchConceptsRecombination-activating gene 1Zinc-binding motifDimerization domainZinc fingerProtein-protein interactionsLymphoid-specific genesN-terminal thirdZinc finger sequencesAmino acid residuesC3HC4 motifRAG1 sequencesRAG1 proteinTerminal domainHomodimer formationAcid residuesBiophysical techniquesGene 1Energetics of associationMonomeric subunitsMotifProteinFinger sequencesSequenceC3HC4Zinc ions
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