2018
Newly synthesized polycystin‐1 takes different trafficking pathways to the apical and ciliary membranes
Gilder AL, Chapin HC, Padovano V, Hueschen CL, Rajendran V, Caplan MJ. Newly synthesized polycystin‐1 takes different trafficking pathways to the apical and ciliary membranes. Traffic 2018, 19: 933-945. PMID: 30125442, PMCID: PMC6237641, DOI: 10.1111/tra.12612.Peer-Reviewed Original ResearchConceptsPolycystin-1Ciliary deliveryBrefeldin AApical deliveryRenal epithelial cellsN-terminal fragmentPolycystin-2LLC-PK1 renal epithelial cellsDifferent trafficking pathwaysTrans-Golgi networkApical membraneEpithelial cellsCultured epithelial cellsTrafficking pathwaysTransmembrane proteinGolgi compartmentPrimary ciliaC-terminal fragmentCiliary membraneC-terminusAutocatalytic cleavageDistinct pathwaysIncubating cellsCell membraneAutosomal dominant polycystic kidney disease
2011
Regulated Intramembrane Proteolysis: Signaling Pathways and Biological Functions
Lal M, Caplan M. Regulated Intramembrane Proteolysis: Signaling Pathways and Biological Functions. Physiology 2011, 26: 34-44. PMID: 21357901, DOI: 10.1152/physiol.00028.2010.Peer-Reviewed Original ResearchConceptsFundamental cellular processesIntegral membrane proteinsFunctional protein domainsCellular processesProtein domainsElicit biological responsesMembrane proteinsTransmembrane proteinIntramembrane cleavageBiological functionsPhysiological processesProteolytic cleavageBiological responsesProteinCleavageDomainMessengerEnzymePathwayMembrane
2003
The COOH-terminal tail of the GAT-2 GABA transporter contains a novel motif that plays a role in basolateral targeting
Brown A, Muth T, Caplan M. The COOH-terminal tail of the GAT-2 GABA transporter contains a novel motif that plays a role in basolateral targeting. American Journal Of Physiology - Cell Physiology 2003, 286: c1071-c1077. PMID: 15075206, DOI: 10.1152/ajpcell.00291.2003.Peer-Reviewed Original ResearchConceptsBasolateral targetingTerminal tailAmino acidsBasolateral distributionPlasma membrane domainsMadin-Darby canine kidney cellsCanine kidney cellsMembrane domainsTransmembrane proteinNovel motifCOOH terminusMolecular signalsAcid transportersGamma-amino butyric acid (GABA) transportersVectorial transportPolar distributionTransportersButyric acid transporterGAT-2Kidney cellsMotifGABA transporterProteinTargetingAsymmetrical distribution
1986
Newly synthesized Na,K-ATPase alpha-subunit has no cytosolic intermediate in MDCK cells.
Caplan MJ, Palade GE, Jamieson JD. Newly synthesized Na,K-ATPase alpha-subunit has no cytosolic intermediate in MDCK cells. Journal Of Biological Chemistry 1986, 261: 2860-2865. PMID: 3005269, DOI: 10.1016/s0021-9258(17)35866-0.Peer-Reviewed Original ResearchConceptsAlpha subunitAnimal cell plasma membranesK-ATPase alpha subunitMDCK cellsMembrane-bound vesiclesCell plasma membraneCytosol fractionTransmembrane proteinCrude cytosolic fractionPlasma membraneMembranous vesiclesPrecursor-product relationshipSoluble precursorsMembrane vesiclesK-ATPaseCytosolic fractionMembrane pelletVesiclesStaphylococcus aureus cellsAureus cellsCellsMonoclonal antibodiesProteinPrecursorsMembrane