2008
The Cytoplasmic Tail Dileucine Motif LL572 Determines the Glycosylation Pattern of Membrane-type 1 Matrix Metalloproteinase*
Ludwig T, Theissen SM, Morton MJ, Caplan MJ. The Cytoplasmic Tail Dileucine Motif LL572 Determines the Glycosylation Pattern of Membrane-type 1 Matrix Metalloproteinase*. Journal Of Biological Chemistry 2008, 283: 35410-35418. PMID: 18955496, PMCID: PMC2602891, DOI: 10.1074/jbc.m801816200.Peer-Reviewed Original ResearchConceptsMT1-MMPMT1-MMP traffickingSite-directed mutagenesis studiesCell surface traffickingMembrane type 1 matrix metalloproteinasePost-translational processingCytoplasmic tailMolecular charactersMutagenesis studiesSurface traffickingMetabolic labelingSubstrate spectrumMatrix metalloproteinaseEnzymatic deglycosylationGlycosylation patternsProfound physiological effectsHinge regionTraffickingPathological processesProteinLectin precipitationPost-synthetic pathwayPhysiological effectsMajor effectBroad spectrumExon Loss Accounts for Differential Sorting of Na-K-Cl Cotransporters in Polarized Epithelial Cells
Carmosino M, Giménez I, Caplan M, Forbush B. Exon Loss Accounts for Differential Sorting of Na-K-Cl Cotransporters in Polarized Epithelial Cells. Molecular Biology Of The Cell 2008, 19: 4341-4351. PMID: 18667527, PMCID: PMC2555935, DOI: 10.1091/mbc.e08-05-0478.Peer-Reviewed Original ResearchConceptsDileucine motifNa-K-Cl cotransporterRenal Na-K-Cl cotransporterPolarized epithelial cellsAmino acid stretchApical proteinsApical sortingEvolutionary lossRenal epithelial cell lineGene structurePhylogenetic analysisDifferential sortingDirect traffickingEpithelial cell lineAdditional exonC-terminusMammalian kidneyApical membraneExonsNovel mechanismNKCC2 geneCell linesBasolateral membraneMotifEpithelial cells
2004
Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression
Duffield A, Fölsch H, Mellman I, Caplan MJ. Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression. Traffic 2004, 5: 449-461. PMID: 15117319, DOI: 10.1111/j.1398-9219.2004.00192.x.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportAmino Acid MotifsAnimalsCell LineCytoplasmDogsEpithelial CellsGlutathione TransferaseH(+)-K(+)-Exchanging ATPaseLLC-PK1 CellsMembrane ProteinsProtein SubunitsProtein TransportReceptors, LDLReceptors, TransferrinRecombinant Fusion ProteinsSwineTransfectionTyrosineConceptsLow-density lipoproteinTransferrin receptorBasolateral localizationTyrosine-based motifMDCK cellsB expressionLLC-PK1 cellsEpithelial cellsLipoproteinMadin-Darby canine kidney cellsCertain epithelial cellsReceptorsKidney cellsCanine kidney cellsK-ATPase beta subunitCellsDifferential expressionK-ATPaseBasolateral expressionExpressionApical membrane
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 ResearchMeSH KeywordsAmino Acid MotifsAnimalsCell LineDogsHomeostasisIntracellular MembranesMembrane Transport ProteinsSignal TransductionConceptsBasolateral 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