2022
SHIP164 is a chorein motif lipid transfer protein that controls endosome–Golgi membrane traffic
Hanna MG, Suen PH, Wu Y, Reinisch KM, De Camilli P. SHIP164 is a chorein motif lipid transfer protein that controls endosome–Golgi membrane traffic. Journal Of Cell Biology 2022, 221: e202111018. PMID: 35499567, PMCID: PMC9067936, DOI: 10.1083/jcb.202111018.Peer-Reviewed Original ResearchConceptsMannose-6-phosphate receptorCation-independent mannose-6-phosphate receptorMembrane contact sitesEarly endocytic pathwayGolgi membrane trafficLipid transfer proteinLipid transfer propertiesProtein-lipid ratioMembrane cargoMembrane trafficEndocytic membranesVesicular trafficRetrograde trafficEndocytic pathwayFunctional characterizationContact sitesMembranous organellesGolgi complexVesicle clustersCellular membranesTransfer proteinProteinLipid compositionOrganellesMembrane
2000
Functional Characterization of a Mammalian Sac1 and Mutants Exhibiting Substrate-specific Defects in Phosphoinositide Phosphatase Activity*
Nemoto Y, Kearns B, Wenk M, Chen H, Mori K, Alb J, De Camilli P, Bankaitis V. Functional Characterization of a Mammalian Sac1 and Mutants Exhibiting Substrate-specific Defects in Phosphoinositide Phosphatase Activity*. Journal Of Biological Chemistry 2000, 275: 34293-34305. PMID: 10887188, DOI: 10.1074/jbc.m003923200.Peer-Reviewed Original ResearchConceptsSubstrate-specific defectsIntegral membrane proteinsPhosphoinositide phosphatase activityPhosphatase activityMembrane proteinsEndoplasmic reticulumGolgi secretory functionIntegral membrane lipidEukaryotic cell physiologyPrimary sequence homologyYeast Sac1pSAC1 geneHeterologous complementationActin functionSac1 domainSac1pBisphosphate substrateMembrane phosphoinositidesPhosphatidylinositol 3Cell physiologyFunctional characterizationGene productsSequence homologyProtein activityGolgi complex