2016
The polycystins are modulated by cellular oxygen-sensing pathways and regulate mitochondrial function
Padovano V, Kuo IY, Stavola LK, Aerni HR, Flaherty BJ, Chapin HC, Ma M, Somlo S, Boletta A, Ehrlich BE, Rinehart J, Caplan MJ. The polycystins are modulated by cellular oxygen-sensing pathways and regulate mitochondrial function. Molecular Biology Of The Cell 2016, 28: 261-269. PMID: 27881662, PMCID: PMC5231895, DOI: 10.1091/mbc.e16-08-0597.Peer-Reviewed Original ResearchConceptsPolycystin-1Polycystin-2Cellular oxygen-sensing pathwaysMitochondrial functionOxygen-sensing pathwayBroad physiological rolesProlyl hydroxylase domainCellular energy metabolismPolycystin complexIon channel complexEndoplasmic reticulum CaPC1 expressionSubcellular localizationHydroxylase domainMitochondrial CaER CaNovel rolePhysiological roleEnergy metabolismChannel complexChannel activityPolycystinsAutosomal dominant polycystic kidney diseaseReticulum CaDominant polycystic kidney disease
2014
Altered trafficking and stability of polycystins underlie polycystic kidney disease
Cai Y, Fedeles SV, Dong K, Anyatonwu G, Onoe T, Mitobe M, Gao JD, Okuhara D, Tian X, Gallagher AR, Tang Z, Xie X, Lalioti MD, Lee AH, Ehrlich BE, Somlo S. Altered trafficking and stability of polycystins underlie polycystic kidney disease. Journal Of Clinical Investigation 2014, 124: 5129-5144. PMID: 25365220, PMCID: PMC4348948, DOI: 10.1172/jci67273.Peer-Reviewed Original ResearchConceptsG-protein-coupled receptor proteolytic sitePolycystic kidney diseaseKidney diseaseGPS cleavageAutosomal dominant polycystic kidney diseaseMissense mutationsDominant polycystic kidney diseasePolycystin-1Polycystin-2Murine modelSevere formPathogenic missense mutationsPKD1 mutationsCOOH-terminal fragmentDiseaseMissense variantsExpression levelsFunctional assaysCell-based systemsAltered trafficking
2012
Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells
Lang S, Benedix J, Fedeles SV, Schorr S, Schirra C, Schäuble N, Jalal C, Greiner M, Haßdenteufel S, Tatzelt J, Kreutzer B, Edelmann L, Krause E, Rettig J, Somlo S, Zimmermann R, Dudek J. Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells. Journal Of Cell Science 2012, 125: 1958-1969. PMID: 22375059, PMCID: PMC4074215, DOI: 10.1242/jcs.096727.Peer-Reviewed Original ResearchConceptsPost-translational transportTail-anchored proteinsSEC61A1 geneEndoplasmic reticulumTransport of polypeptidesCo-translational transportSemi-permeabilized cellsPrecursor proteinSEC62 geneSec61 channelPresecretory proteinsMembrane integrationProtein transportMammalian cellsKnockdown approachHuman cellsGenesHeLa cellsProteinPolypeptideReticulumCellsSec63pSec61αSec63