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
The 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