2001
Distinction between signaling mechanisms in lipid rafts vs. caveolae
Sowa G, Pypaert M, Sessa W. Distinction between signaling mechanisms in lipid rafts vs. caveolae. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 14072-14077. PMID: 11707586, PMCID: PMC61169, DOI: 10.1073/pnas.241409998.Peer-Reviewed Original ResearchConceptsCav-1Raft domainsLipid raftsCholesterol-rich lipid raft domainsLipid raft domainsCaveolae assemblyEndothelial nitric oxide synthaseCaveolae biogenesisAcylated proteinsSignal transductionSpatial regulationPlasma membraneNegative regulationCaveolin-1CaveolaeFirst clear exampleRaftsPhysical interactionProteinCellsRegulationENOS functionBiogenesisDomainClear example
2000
Reconstitution of an Endothelial Nitric-oxide Synthase (eNOS), hsp90, and Caveolin-1 Complex in Vitro EVIDENCE THAT hsp90 FACILITATES CALMODULIN STIMULATED DISPLACEMENT OF eNOS FROM CAVEOLIN-1*
Gratton J, Fontana J, O'Connor D, Garcı́a-Cardeña G, McCabe T, Sessa W. Reconstitution of an Endothelial Nitric-oxide Synthase (eNOS), hsp90, and Caveolin-1 Complex in Vitro EVIDENCE THAT hsp90 FACILITATES CALMODULIN STIMULATED DISPLACEMENT OF eNOS FROM CAVEOLIN-1*. Journal Of Biological Chemistry 2000, 275: 22268-22272. PMID: 10781589, DOI: 10.1074/jbc.m001644200.Peer-Reviewed Original ResearchConceptsEndothelial nitric oxide synthaseAssociation of eNOSNitric oxide synthaseLung microvascular endothelial cellsCaveolin-1Microvascular endothelial cellsENOS enzymatic activityAction of CaMBovine lung microvascular endothelial cellsENOS functionCalcium-activated calmodulinConcentration of CaMShock protein 90Addition of CaMEndothelial cellsVitro EvidenceCav-1Protein 90AssociationPresence of Hsp90