2024
Structural bases for Na+-Cl− cotransporter inhibition by thiazide diuretic drugs and activation by kinases
Zhao Y, Schubert H, Blakely A, Forbush B, Smith M, Rinehart J, Cao E. Structural bases for Na+-Cl− cotransporter inhibition by thiazide diuretic drugs and activation by kinases. Nature Communications 2024, 15: 7006. PMID: 39143061, PMCID: PMC11324901, DOI: 10.1038/s41467-024-51381-y.Peer-Reviewed Original ResearchConceptsNa+-Cl- cotransporterFamilial hyperkalemic hypertensionRenal salt retentionThiazide diuretic drugsNa+-Cl-Cotransporter inhibitionNCC activitySalt reabsorptionDiuretic drugsBlood pressureBalanced electrolyteTreat hypertensionIon translocation pathwayIon translocationThiazideHypertensionSalt retentionOrthosteric siteCo-structureCarboxyl-terminal domainKinase cascadeEdemaChlorthalidoneCotransporterTranslocation
2015
The PINK1-PARKIN Mitochondrial Ubiquitylation Pathway Drives a Program of OPTN/NDP52 Recruitment and TBK1 Activation to Promote Mitophagy
Heo JM, Ordureau A, Paulo JA, Rinehart J, Harper JW. The PINK1-PARKIN Mitochondrial Ubiquitylation Pathway Drives a Program of OPTN/NDP52 Recruitment and TBK1 Activation to Promote Mitophagy. Molecular Cell 2015, 60: 7-20. PMID: 26365381, PMCID: PMC4592482, DOI: 10.1016/j.molcel.2015.08.016.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingCell Cycle ProteinsHeLa CellsHumansMembrane Transport ProteinsMitochondriaMitophagyNuclear ProteinsPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProteomicsSequestosome-1 ProteinTranscription Factor TFIIIAUbiquitin-Protein LigasesUbiquitinationConceptsUbiquitin chainsEfficient mitophagyTBK1 activationPINK1-Parkin pathwayUbiquitylation pathwayAdaptor recruitmentCellular homeostasisMitochondrial retentionTBK1 kinaseDamaged mitochondriaChain bindingMitophagyHeLa cellsMitochondriaPhosphorylationNDP52Positive feedback mechanismPathwayOPTNRecruitmentActivationAmyotrophic lateral sclerosisAssemblyS473Kinase