2016
C9orf72 binds SMCR8, localizes to lysosomes, and regulates mTORC1 signaling
Amick J, Roczniak-Ferguson A, Ferguson SM. C9orf72 binds SMCR8, localizes to lysosomes, and regulates mTORC1 signaling. Molecular Biology Of The Cell 2016, 27: 3040-3051. PMID: 27559131, PMCID: PMC5063613, DOI: 10.1091/mbc.e16-01-0003.Peer-Reviewed Original ResearchConceptsAmino acid availabilityAcid availabilityGenome-editing strategiesKO cell linesProtein complexesSubcellular localizationKnockout phenotypesC9orf72 proteinLysosomal siteBioinformatics predictionSMCR8Tumor suppressorSwollen lysosomesFunctional interactionLysosomesC9orf72 geneCell linesStructural similarityNormal functionC9orf72PhenotypeAmyotrophic lateral sclerosisBirt-HoggIntronsMTORC1
2013
Recruitment of folliculin to lysosomes supports the amino acid–dependent activation of Rag GTPases
Petit CS, Roczniak-Ferguson A, Ferguson SM. Recruitment of folliculin to lysosomes supports the amino acid–dependent activation of Rag GTPases. Journal Of Cell Biology 2013, 202: 1107-1122. PMID: 24081491, PMCID: PMC3787382, DOI: 10.1083/jcb.201307084.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsBlotting, WesternCarrier ProteinsCytoplasmFluorescent Antibody TechniqueHumansImmunoprecipitationLysosomesMechanistic Target of Rapamycin Complex 1Monomeric GTP-Binding ProteinsMultiprotein ComplexesProto-Oncogene ProteinsRecombinant ProteinsRNA, Small InterferingTOR Serine-Threonine KinasesTumor Suppressor ProteinsConceptsAmino acid-dependent activationAcid-dependent activationTranscription factor EBRag GTPasesSurface of lysosomesMTORC1-dependent phosphorylationAmino acid depletionLysosome recruitmentGTPase domainRAG interactionsCytoplasmic sequestrationLysosome functionGTPasesFLCNHuman diseasesFunction mutationsDevelopment of pneumothoraxProtein 1Direct interactionLysosomesCritical rolePulmonary cystsSite of actionAcid depletionFolliculin gene
1996
Nitric oxide stimulates guanylate cyclase and regulates sodium transport in rabbit proximal tubule
Roczniak A, Burns K. Nitric oxide stimulates guanylate cyclase and regulates sodium transport in rabbit proximal tubule. American Journal Of Physiology 1996, 270: f106-f115. PMID: 8769828, DOI: 10.1152/ajprenal.1996.270.1.f106.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportCarrier ProteinsCells, CulturedCyclic AMP-Dependent Protein KinasesCyclic GMPEnzyme ActivationFemaleGuanylate CyclaseKidney Tubules, ProximalNitric OxideNitroprussidePenicillamineRabbitsS-Nitroso-N-AcetylpenicillamineSodiumSodium-Hydrogen ExchangersSodium-Phosphate Cotransporter ProteinsSymportersConceptsS-nitroso-N-acetylpenicillamineProximal tubule cellsRabbit proximal tubuleSoluble guanylate cyclaseProtein kinase AProximal tubulesSodium nitroprussideNa+/H+ exchangeTubule cellsGuanylate cyclaseNitric oxidePrimary cultures of proximal tubule cellsAmiloride-sensitive 22Na+ uptakeNa+ transportInhibitor of soluble guanylate cyclaseFractional excretion of lithiumRabbit proximal tubule cellsApical Na+/H+ exchangerGuanosine 3',5'-cyclic monophosphateStable end-products of NOEnd-products of NORegulating sodium transportNO stimulates soluble guanylate cyclaseEffects of NO donorsDose-dependent increase