2003
Phosphoinositide Recognition Domains
Lemmon MA. Phosphoinositide Recognition Domains. Traffic 2003, 4: 201-213. PMID: 12694559, DOI: 10.1034/j.1600-0854.2004.00071.x.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainPhox homologyHomology domainEpsin ENTH domainENTH domainMembrane recruitmentFYVE domainBind phosphoinositidesTargeting domainsCellular phosphoinositidesCellular signalingCytoskeletal remodelingLipid bindingIntracellular traffickingStructural basisDistinct functionsExquisite specificityRecognition domainPhosphoinositideSpecificity characteristicsBilayer curvatureSignificant insightsHigh affinityDomainHomology
1999
Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
Takei K, Slepnev V, Haucke V, De Camilli P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nature Cell Biology 1999, 1: 33-39. PMID: 10559861, DOI: 10.1038/9004.Peer-Reviewed Original ResearchConceptsDynamin 1Functional partnershipCell-free systemAmphiphysin 1Clathrin coatDynaminAmphiphysinRing-like structurePresence of GTPSynaptic vesiclesEndocytosisNarrow tubulesLipid bilayersMorphological evidenceBilayer curvatureVesiclesSpherical liposomesPotential functionClathrinGTPDirect morphological evidenceProteinAssembles
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