2014
Sac1–Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus
Cai Y, Deng Y, Horenkamp F, Reinisch KM, Burd CG. Sac1–Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus. Journal Of Cell Biology 2014, 206: 485-491. PMID: 25113029, PMCID: PMC4137058, DOI: 10.1083/jcb.201404041.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsCatalysisCrystallography, X-RayEndoplasmic ReticulumGolgi ApparatusGreen Fluorescent ProteinsMembrane ProteinsModels, MolecularMultiprotein ComplexesPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsGolgi apparatusHomology domainRegulation of phosphatidylinositolN-terminal subdomainN-terminal portionPhosphoinositide phosphataseFamily proteinsSignal terminationEndoplasmic reticulumPhosphatidylinositolMembrane compositionSAC1Dual functionPhosphoinositideEffectorsPhosphataseAmyotrophic lateral sclerosisCharcot-MarieBroad distributionVps74OrthologuesTooth disordersGOLPH3MannosyltransferaseLateral sclerosis
2010
Structure and function of the polymerase core of TRAMP, a RNA surveillance complex
Hamill S, Wolin SL, Reinisch KM. Structure and function of the polymerase core of TRAMP, a RNA surveillance complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 15045-15050. PMID: 20696927, PMCID: PMC2930566, DOI: 10.1073/pnas.1003505107.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceBase SequenceBinding SitesCrystallography, X-RayDNA-Directed DNA PolymeraseModels, MolecularMolecular Sequence DataMultiprotein ComplexesProtein Interaction Domains and MotifsRecombinant ProteinsRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidStatic ElectricitySubstrate SpecificityConceptsZinc knuckle motifHigher eukaryotesSubstrate recognitionRNA polymeraseCentral domainInitial substrate recognitionRNA 3' endsTRAMP complexRNA surveillanceZinc knuckleCharacterized enzymesAberrant RNAsSurveillance complexPolymerase coreRNA bindingAir2pNucleotidyl transferaseTrf4pN-terminusEukaryotesInteraction surfacePolymeraseMotifNucleic acidsComplexesStructure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes
Vasan N, Hutagalung A, Novick P, Reinisch KM. Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 14176-14181. PMID: 20660722, PMCID: PMC2922553, DOI: 10.1073/pnas.1009419107.Peer-Reviewed Original ResearchConceptsGolgi-associated retrograde proteinC-terminusC-terminal fragmentGolgi-associated retrograde protein (GARP) complexCommon evolutionary originAlpha-helical bundleTrans-Golgi networkEndosome-derived vesiclesMembrane trafficVesicle recognitionEvolutionary originProtein complexesOligomeric GolgiTerminusSubunitsProteinComplexesDsl1ExocystFragmentsEndosomesGolgiFamilyMutationsVesicles