2008
An Internal Domain of Exo70p Is Required for Actin-independent Localization and Mediates Assembly of Specific Exocyst Components
Hutagalung A, Coleman J, Pypaert M, Novick P. An Internal Domain of Exo70p Is Required for Actin-independent Localization and Mediates Assembly of Specific Exocyst Components. Molecular Biology Of The Cell 2008, 20: 153-163. PMID: 18946089, PMCID: PMC2613103, DOI: 10.1091/mbc.e08-02-0157.Peer-Reviewed Original ResearchMeSH KeywordsActinsAmino Acid SequenceCell MembraneExocytosisModels, MolecularMolecular Sequence DataMutationProtein Structure, TertiaryProtein SubunitsRecombinant Fusion ProteinsRho GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory PathwayVesicular Transport ProteinsConceptsExocyst assemblyPlasma membraneHigh copy number suppressorActin-independent pathwayAmino-terminal domainSynthetic lethal interactionsRod-shaped subunitsNumber suppressorVesicle tethersExocyst componentsExocytic sitesActin cablesExo70pSingle geneSecretory vesiclesLethal interactionsSec3pSynthetic lethalityComplete deletionExocystInternal domainSubunitsDeletionMutationsVesicles
2006
Rtn1p Is Involved in Structuring the Cortical Endoplasmic Reticulum
De Craene J, Coleman J, Estrada de Martin P, Pypaert M, Anderson S, Yates J, Ferro-Novick S, Novick P. Rtn1p Is Involved in Structuring the Cortical Endoplasmic Reticulum. Molecular Biology Of The Cell 2006, 17: 3009-3020. PMID: 16624861, PMCID: PMC1483037, DOI: 10.1091/mbc.e06-01-0080.Peer-Reviewed Original ResearchConceptsCortical endoplasmic reticulumEndoplasmic reticulumNuclear envelopeCortical ER networkReticular endoplasmic reticulumMembrane-spanning domainsExocyst functionYeast mutantsProtein associatesBud tipProteomic screenYeast budER morphologyCell cortexHydrophilic loopSystematic screenSecretory vesiclesRtn1pER structureER networkExocystProteinModest accumulationReticulumOverexpressionThe rab Exchange Factor Sec2p Reversibly Associates with the Exocyst
Medkova M, France Y, Coleman J, Novick P. The rab Exchange Factor Sec2p Reversibly Associates with the Exocyst. Molecular Biology Of The Cell 2006, 17: 2757-2769. PMID: 16611746, PMCID: PMC1474791, DOI: 10.1091/mbc.e05-10-0917.Peer-Reviewed Original ResearchConceptsSecretory vesiclesExchange factor Sec2pTemperature-sensitive growthC-terminal halfExocyst complexExocytic sitesRab GTPaseExchange factorMutant resultsMutant correlatesRecycling pathwaySec2pExocystNucleotide exchangePlasma membraneSec4pSec15pVesiclesMislocalizationEffectorsPolarized transportAssociatesGTPaseExocytosisPathwayThe polarity-establishment component Bem1p interacts with the exocyst complex through the Sec15p subunit
France Y, Boyd C, Coleman J, Novick P. The polarity-establishment component Bem1p interacts with the exocyst complex through the Sec15p subunit. Journal Of Cell Science 2006, 119: 876-888. PMID: 16478783, DOI: 10.1242/jcs.02849.Peer-Reviewed Original ResearchConceptsBud growthSrc homology 3 domainTwo-hybrid studiesFirst Src homology 3 domainDirect physical interactionGreen fluorescent proteinExocyst complexGolgi traffickingSec15pSecretory pathwaySpatial regulationBem1pSecretory machineryMaster regulatorFluorescent proteinNew budsMachineryExocystSec4pPhysical interactionSubunitsCase of cellsProteinPathwayCrucial role