Seong An, PhD
Senior Research Scientist in PharmacologyCards
Contact Info
Education
PhD
University of Cambridge, Pharmacology (1999)
University of Cambridge, Pharmacology (1999)
BA
Yale University, Molecular Biophysics & Biochemistry (1994)
Yale University, Molecular Biophysics & Biochemistry (1994)
About
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Titles
Senior Research Scientist in Pharmacology
Appointments
Pharmacology
Senior Research ScientistPrimary
Other Departments & Organizations
Education & Training
- PhD
- University of Cambridge, Pharmacology (1999)
- BA
- Yale University, Molecular Biophysics & Biochemistry (1994)
Research
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Research at a Glance
Yale Co-Authors
Frequent collaborators of Seong An's published research.
Publications Timeline
A big-picture view of Seong An's research output by year.
Francisco Tome
Sangwon Lee, PhD
Yoshihisa Suzuki
Pietro De Camilli, MD
Stephen Strittmatter, MD, PhD, AB
Wenxue Li
6Publications
132Citations
Publications
2024
Modulation of FGF pathway signaling and vascular differentiation using designed oligomeric assemblies
Edman N, Phal A, Redler R, Schlichthaerle T, Srivatsan S, Ehnes D, Etemadi A, An S, Favor A, Li Z, Praetorius F, Gordon M, Vincent T, Marchiano S, Blakely L, Lin C, Yang W, Coventry B, Hicks D, Cao L, Bethel N, Heine P, Murray A, Gerben S, Carter L, Miranda M, Negahdari B, Lee S, Trapnell C, Zheng Y, Murry C, Schweppe D, Freedman B, Stewart L, Ekiert D, Schlessinger J, Shendure J, Bhabha G, Ruohola-Baker H, Baker D. Modulation of FGF pathway signaling and vascular differentiation using designed oligomeric assemblies. Cell 2024, 187: 3726-3740.e43. PMID: 38861993, PMCID: PMC11246234, DOI: 10.1016/j.cell.2024.05.025.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsIntracellular tyrosine kinase domainMitogen-activated protein kinase (MAPK) pathway activationDownstream signaling cascadesCyclic homo-oligomersTyrosine kinase domainReceptor valencyCell fateOligomeric assembliesKinase domainSignaling outcomesSignaling ligandsHomo-oligomersSplice variantsSignaling cascadesCytokine signalingExtracellular domainPathway signalingDevelopmental transitionsProtein building blocksVascular differentiationPathway activationVascular developmentComplexity of signalsModular assemblyTherapeutic applications
2023
Heparin is essential for optimal cell signaling by FGF21 and for regulation of βKlotho cellular stability
An S, Mohanty J, Tome F, Suzuki Y, Lax I, Schlessinger J. Heparin is essential for optimal cell signaling by FGF21 and for regulation of βKlotho cellular stability. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2219128120. PMID: 36745784, PMCID: PMC9962926, DOI: 10.1073/pnas.2219128120.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsHeparan sulfate proteoglycanCellular stabilityCell membraneSingle-molecule fluorescenceProtein kinase responsesChinese hamster ovary cellsFGF moleculesHamster ovary cellsFactor bindsReceptor assemblyReceptor dimerizationGrowth factor bindsHigh-affinity bindingFGF1 stimulationKinase responseCHO cellsOvary cellsSulfate proteoglycanIntracellular CaKlotho proteinFGFR1cPotential roleRegulationΒKlothoCells
2022
Regulation of EGF-stimulated activation of the PI-3K/AKT pathway by exocyst-mediated exocytosis
An S, Anneken A, Xi Z, Choi C, Schlessinger J, Toomre D. Regulation of EGF-stimulated activation of the PI-3K/AKT pathway by exocyst-mediated exocytosis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2208947119. PMID: 36417441, PMCID: PMC9860279, DOI: 10.1073/pnas.2208947119.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsPI-3K/Akt pathwayAkt pathwayAkt activationDocking protein Gab1EGF-stimulated activationEpithelial cellsLive-cell imagingPhosphoinositide-3 kinaseCell survival pathwaysExocyst complexExocyst functionSmall molecule inhibitorsVesicle tethersExocytic fusionProtein Gab1EGF stimulationExocystSurvival pathwaysExocytosisInhibitors resultsPathwayImportant pathwayEGFR inhibitionMinute time scaleVesiclesMultimodal imaging of synaptic vesicles with a single probe
An SJ, Stagi M, Gould TJ, Wu Y, Mlodzianoski M, Rivera-Molina F, Toomre D, Strittmatter SM, De Camilli P, Bewersdorf J, Zenisek D. Multimodal imaging of synaptic vesicles with a single probe. Cell Reports Methods 2022, 2: 100199. PMID: 35497490, PMCID: PMC9046237, DOI: 10.1016/j.crmeth.2022.100199.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsC2 domainSynaptic vesiclesSynaptic vesicle recyclingMembrane-binding C2 domainMultiple microscopy methodsEndocytic markersMembrane recyclingVesicle functionVesicle populationsCytosolic phospholipase ACell typesPhospholipase ADetectable tagMicroscopy modalitiesModular probesMultiple microscopy techniquesVesiclesComplete understandingDomainMicroscopy methodsMultiple levelsProbeAvailable probesMicroscopy techniquesPathway
2021
An active tethering mechanism controls the fate of vesicles
An SJ, Rivera-Molina F, Anneken A, Xi Z, McNellis B, Polejaev VI, Toomre D. An active tethering mechanism controls the fate of vesicles. Nature Communications 2021, 12: 5434. PMID: 34521845, PMCID: PMC8440521, DOI: 10.1038/s41467-021-25465-y.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsArtificial tetherFull fusionOptogenetic controlExocyst complexExocyst functionVesicle tethersMembrane mergerTethering mechanismTarget membraneIntracellular fusionPlasma membraneMode of fusionVesicle fusionPhysiological relevanceLamellipodial expansionVesiclesTetheringExocystMembraneFusionFurther showTetherFusion modeFateComplexes
2020
FGF23 contains two distinct high-affinity binding sites enabling bivalent interactions with α-Klotho
Suzuki Y, Kuzina E, An SJ, Tome F, Mohanty J, Li W, Lee S, Liu Y, Lax I, Schlessinger J. FGF23 contains two distinct high-affinity binding sites enabling bivalent interactions with α-Klotho. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 31800-31807. PMID: 33257569, PMCID: PMC7749347, DOI: 10.1073/pnas.2018554117.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsMeSH KeywordsBinding SitesCalcinosisCell MembraneFibroblast Growth Factor-23Fibroblast Growth FactorsGlucuronidaseHEK293 CellsHumansHyperostosis, Cortical, CongenitalHyperphosphatemiaImmunoglobulin Fc FragmentsKlotho ProteinsMutationOsteomalaciaProtein BindingProtein DomainsProtein MultimerizationRecombinant Fusion ProteinsRickets, HypophosphatemicConceptsFGF receptorsTotal internal reflection fluorescence microscopyChimeric receptor moleculesReflection fluorescence microscopyBinding sitesDisulfide bridge formationCritical metabolic processesMAPK responseCytoplasmic domainGrowth factor familyTerminal tailFactor familyKinase activationSimilar binding affinitiesExtracellular domainFGFR1 activationTandem repeatsMetabolic processesDisulfide bridgesCell surfaceDistinct ligandsCell membraneFluorescence microscopyDistinct high-affinity binding sitesPhosphate homeostasis
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