2024
Structure, interaction and nervous connectivity of beta cell primary cilia
Müller A, Klena N, Pang S, Garcia L, Topcheva O, Aurrecoechea Duran S, Sulaymankhil D, Seliskar M, Mziaut H, Schöniger E, Friedland D, Kipke N, Kretschmar S, Münster C, Weitz J, Distler M, Kurth T, Schmidt D, Hess H, Xu C, Pigino G, Solimena M. Structure, interaction and nervous connectivity of beta cell primary cilia. Nature Communications 2024, 15: 9168. PMID: 39448638, PMCID: PMC11502866, DOI: 10.1038/s41467-024-53348-5.Peer-Reviewed Original ResearchConceptsPrimary ciliaCell's primary ciliumNon-islet cellsPancreatic beta cellsCiliary pocketSensory organellesAxonemal organizationMotility componentsExtrinsic signalsStructural basisBeta cellsCiliaCell typesExpansion microscopyParacrine signalingIslet innervationCellsIsletsBetaAxonemeOrganellesSignalThree-dimensional reconstructionInteraction
2012
Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein
Heuser T, Barber CF, Lin J, Krell J, Rebesco M, Porter ME, Nicastro D. Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: e2067-e2076. PMID: 22733763, PMCID: PMC3409752, DOI: 10.1073/pnas.1120690109.Peer-Reviewed Original ResearchConceptsI1 dyneinCryoelectron tomographyGel-based proteomicsInner arm dyneinsCiliary assemblySensory organellesSubtomogram averagingDynein activityCritical regulatorDyneinPolypeptide compositionDoublet microtubulesBiochemical comparisonMotor domainCiliary motilityFlagellar beatingUnique interactionsCiliary beatingMotilityEukaryotesAssemblyChlamydomonasSubcomplexMutantsCiliopathies
2011
Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases
Choi YH, Suzuki A, Hajarnis S, Ma Z, Chapin HC, Caplan MJ, Pontoglio M, Somlo S, Igarashi P. Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 10679-10684. PMID: 21670265, PMCID: PMC3127890, DOI: 10.1073/pnas.1016214108.Peer-Reviewed Original ResearchConceptsPolycystin-2Primary ciliaA-kinase anchoring protein 150Dysregulation of cAMPTranscription factor hepatocyte nuclear factor-1βCystic kidney diseasePolycystic kidney diseaseCAMP levelsAKAP complexesRenal primary ciliaRenal epithelial cellsProtein complexesSensory organellesHuman polycystic kidney diseaseC-terminusProtein 150Hepatocyte nuclear factor-1βCalcium channel activityCell surfaceChannel activityCiliaKidney cystsKidney cellsDifferent gene mutationsEpithelial cellsA cell‐based screen for inhibitors of flagella‐driven motility in Chlamydomonas reveals a novel modulator of ciliary length and retrograde actin flow
Engel BD, Ishikawa H, Feldman JL, Wilson CW, Chuang P, Snedecor J, Williams J, Sun Z, Marshall WF. A cell‐based screen for inhibitors of flagella‐driven motility in Chlamydomonas reveals a novel modulator of ciliary length and retrograde actin flow. Cytoskeleton 2011, 68: 188-203. PMID: 21360831, DOI: 10.1002/cm.20504.Peer-Reviewed Original ResearchConceptsRetrograde actin flowActin flowUnicellular green alga Chlamydomonas reinhardtiiGreen alga Chlamydomonas reinhardtiiFlagella-driven motilityDrosophila S2 cellsAlga Chlamydomonas reinhardtiiTraditional genetic methodsChemical biology toolkitCell-based screenHuman disease symptomsLength of ciliaCiliary assemblyFlagellar paralysisS2 cellsIntraflagellar transportGenetic toolsFlagellar shorteningChlamydomonas reinhardtiiMammalian cellsSensory organellesGenetic methodsCiliary lengthCiliary defectsNovel modulator
2008
Zebrafish Tsc1 reveals functional interactions between the cilium and the TOR pathway
DiBella LM, Park A, Sun Z. Zebrafish Tsc1 reveals functional interactions between the cilium and the TOR pathway. Human Molecular Genetics 2008, 18: 595-606. PMID: 19008302, PMCID: PMC2722215, DOI: 10.1093/hmg/ddn384.Peer-Reviewed Original ResearchConceptsKidney cyst formationTOR pathwayCiliary mutantsLeft-right asymmetry defectsVertebrate body planCell surface organellesMultiple signaling pathwaysElongation of ciliaLeft-right asymmetryMorpholino knockdownVertebrate cellsAsymmetry defectsBody planCiliary genesEnvironmental signalsCyst formationKnockdown animalsSensory organellesCilia functionSurface organellesCiliary signalsProtein productsSignaling pathwaysSame pathwayWnt pathwayCystic Kidney Gene seahorse Regulates Cilia-Mediated Processes and Wnt Pathways
Kishimoto N, Cao Y, Park A, Sun Z. Cystic Kidney Gene seahorse Regulates Cilia-Mediated Processes and Wnt Pathways. Developmental Cell 2008, 14: 954-961. PMID: 18539122, DOI: 10.1016/j.devcel.2008.03.010.Peer-Reviewed Original ResearchConceptsWnt pathwayCiliary signalsImportant sensory organelleKidney cyst formationNoncanonical Wnt pathwayCanonical Wnt pathwayLeft-right asymmetryCilia assemblySensory organellesCiliated tissuesCellular eventsCell typesSeahorsesCiliary functionPathwayCiliaCyst formationDishevelledInversinGastrulationVertebratesOrganellesTranscriptsProteinCascade
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