2014
Diversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivation
Langemeyer L, Bastos R, Cai Y, Itzen A, Reinisch KM, Barr FA. Diversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivation. ELife 2014, 3: e01623. PMID: 24520163, PMCID: PMC3919270, DOI: 10.7554/elife.01623.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAspartic AcidBacterial ProteinsCatalytic DomainDeath Domain Receptor Signaling Adaptor ProteinsDNA-Binding ProteinsEnzyme ActivationGlutamineGuanine Nucleotide Exchange FactorsHeLa CellsHumansHydrolysisListeriaModels, MolecularMutagenesis, Site-DirectedMutationProtein ConformationRab GTP-Binding ProteinsRab1 GTP-Binding ProteinsRab5 GTP-Binding ProteinsSignal TransductionTransfectionConceptsActive site residuesGTP hydrolysis mechanismNucleotide-free formActive site glutamineSwitch II regionDifferent RabsRab activationRab GTPasesGTPase activationGlutamine mutantNucleotide exchangeGDP releaseRabActivation mechanismActivation pathwayActive formPathwayResiduesActivationII regionRAPlasticityGTPasesRab5GEF
2008
The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes
Cai Y, Chin HF, Lazarova D, Menon S, Fu C, Cai H, Sclafani A, Rodgers DW, De La Cruz EM, Ferro-Novick S, Reinisch KM. The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes. Cell 2008, 133: 1202-1213. PMID: 18585354, PMCID: PMC2465810, DOI: 10.1016/j.cell.2008.04.049.Peer-Reviewed Original Research