Featured Publications
An optogenetic-phosphoproteomic study reveals dynamic Akt1 signaling profiles in endothelial cells
Zhou W, Li W, Wang S, Salovska B, Hu Z, Tao B, Di Y, Punyamurtula U, Turk B, Sessa W, Liu Y. An optogenetic-phosphoproteomic study reveals dynamic Akt1 signaling profiles in endothelial cells. Nature Communications 2023, 14: 3803. PMID: 37365174, PMCID: PMC10293293, DOI: 10.1038/s41467-023-39514-1.Peer-Reviewed Original ResearchConceptsPhosphorylation sitesSerine/threonine kinase AktMass spectrometry-based phosphoproteomicsThreonine kinase AktAkt-dependent phosphorylationAberrant Akt activationEndothelial cellsKinase substrateKinase AktCell signalingPhosphorylation profilePhenotypic outcomesDownstream signalingAkt activationAkt1 phosphorylationHuman diseasesSystem-level analysisAKT1Vascular endothelial cellsRich resourcePhosphorylationSignalingGrowth factorAktCellsOncogene-like addiction to aneuploidy in human cancers
Girish V, Lakhani A, Thompson S, Scaduto C, Brown L, Hagenson R, Sausville E, Mendelson B, Kandikuppa P, Lukow D, Yuan M, Stevens E, Lee S, Schukken K, Akalu S, Vasudevan A, Zou C, Salovska B, Li W, Smith J, Taylor A, Martienssen R, Liu Y, Sun R, Sheltzer J. Oncogene-like addiction to aneuploidy in human cancers. Science 2023, 381: eadg4521. PMID: 37410869, PMCID: PMC10753973, DOI: 10.1126/science.adg4521.Peer-Reviewed Original ResearchMulti-omic measurements of heterogeneity in HeLa cells across laboratories
Liu Y, Mi Y, Mueller T, Kreibich S, Williams EG, Van Drogen A, Borel C, Frank M, Germain PL, Bludau I, Mehnert M, Seifert M, Emmenlauer M, Sorg I, Bezrukov F, Bena FS, Zhou H, Dehio C, Testa G, Saez-Rodriguez J, Antonarakis SE, Hardt WD, Aebersold R. Multi-omic measurements of heterogeneity in HeLa cells across laboratories. Nature Biotechnology 2019, 37: 314-322. PMID: 30778230, DOI: 10.1038/s41587-019-0037-y.Peer-Reviewed Original ResearchConceptsCell linesGenome-wide copy numberMulti-omic measurementsHuman cultured cellsProtein turnover ratesPhenotypic responsesGenomic variabilityDifferent cell linesHeLa variantsSpecific cell linesCopy numberHeLa cellsCultured cellsHeLa cell linePhenotypic variabilityProgressive divergenceTurnover rateCellsBiological variationTechnical variationUniform conditionsTranscriptomeProteomeSuccessive passagesLines
2021
MAL2 mediates the formation of stable HER2 signaling complexes within lipid raft-rich membrane protrusions in breast cancer cells
Jeong J, Shin JH, Li W, Hong JY, Lim J, Hwang JY, Chung JJ, Yan Q, Liu Y, Choi J, Wysolmerski J. MAL2 mediates the formation of stable HER2 signaling complexes within lipid raft-rich membrane protrusions in breast cancer cells. Cell Reports 2021, 37: 110160. PMID: 34965434, PMCID: PMC8762588, DOI: 10.1016/j.celrep.2021.110160.Peer-Reviewed Original ResearchMeSH KeywordsAntineoplastic Agents, ImmunologicalBreast NeoplasmsCell ProliferationCytoskeletal ProteinsDrug Resistance, NeoplasmEndocytosisFemaleHumansMembrane MicrodomainsMyelin and Lymphocyte-Associated Proteolipid ProteinsPhosphoproteinsPlasma Membrane Calcium-Transporting ATPasesReceptor, ErbB-2Sodium-Hydrogen ExchangersTrastuzumabTumor Cells, CulturedConceptsLipid raft formationBreast cancer cellsLipid raftsLipid raft resident proteinsCancer cellsRaft formationRaft-resident proteinsProximity ligation assayProtein complexesMembrane protrusionsProtein interactionsPlasma membraneLigation assayMAL2Membrane stabilityStructural organizationPotential therapeutic targetPhysical interactionMembrane retentionProteinRaftsTherapeutic targetCellsIntracellular calcium concentrationLow intracellular calcium concentrationA PKD-MFF signaling axis couples mitochondrial fission to mitotic progression
Pangou E, Bielska O, Guerber L, Schmucker S, Agote-Arán A, Ye T, Liao Y, Puig-Gamez M, Grandgirard E, Kleiss C, Liu Y, Compe E, Zhang Z, Aebersold R, Ricci R, Sumara I. A PKD-MFF signaling axis couples mitochondrial fission to mitotic progression. Cell Reports 2021, 35: 109129. PMID: 34010649, DOI: 10.1016/j.celrep.2021.109129.Peer-Reviewed Original ResearchConceptsMitochondrial fission factorProtein kinase DMitochondrial fissionMitotic progressionMFF-dependent mitochondrial fissionGenome integrityChromosome segregationDynamic organellesKinase DMitochondrial receptorDaughter cellsFission factorMammalian cellsMitotic checkpointCell divisionFusion eventsInterphasic cellsCell survivalProtein 1PhosphorylationMitochondriaCellsFissionDynaminOrganelles
2020
A Global Screen for Assembly State Changes of the Mitotic Proteome by SEC-SWATH-MS
Heusel M, Frank M, Köhler M, Amon S, Frommelt F, Rosenberger G, Bludau I, Aulakh S, Linder MI, Liu Y, Collins BC, Gstaiger M, Kutay U, Aebersold R. A Global Screen for Assembly State Changes of the Mitotic Proteome by SEC-SWATH-MS. Cell Systems 2020, 10: 133-155.e6. PMID: 32027860, PMCID: PMC7042714, DOI: 10.1016/j.cels.2020.01.001.Peer-Reviewed Original ResearchConceptsSEC-SWATHHundreds of complexesThousands of proteinsAssembly state changesMitotic proteomeProtein complexesProteomic studiesGlobal screenHuman cellsComplex remodelingHigher-level organizationBiological researchKey hallmarksBiochemical reactionsInteractive exploration toolProteinFunctional stateSpecific changesComplexesProteomeCellsMitosisHallmarkRemodelingInterphase
2016
Deep Phosphoproteomic Measurements Pinpointing Drug Induced Protective Mechanisms in Neuronal Cells
Yu C, Gao J, Zhou Y, Chen X, Xiao R, Zheng J, Liu Y, Zhou H. Deep Phosphoproteomic Measurements Pinpointing Drug Induced Protective Mechanisms in Neuronal Cells. Frontiers In Physiology 2016, 7: 635. PMID: 28066266, PMCID: PMC5179568, DOI: 10.3389/fphys.2016.00635.Peer-Reviewed Original ResearchAlzheimer's diseaseNeuro-2a cellsTau protein phosphorylationIrreversible neurological disordersDrug effectsNeurological disordersNeuronal cellsOlder populationClass IProtective mechanismPhosphorylation levelsNeuron systemDrug candidatesOxidative damageDiseaseMolecular mechanismsCellsInflammationQuantitative phosphoproteomeSILAC labelingPhosphoproteomic approachPhosphorylation changesNOS1PhosphorylationMiceThe interdependence of transcript and protein abundance: new data–new complexities
Liu Y, Aebersold R. The interdependence of transcript and protein abundance: new data–new complexities. Molecular Systems Biology 2016, 12: 856. PMID: 26792872, PMCID: PMC4731012, DOI: 10.15252/msb.20156720.Peer-Reviewed Original ResearchProtein abundanceGene expression controlER stress responseExpression controlTranslational regulationEndoplasmic reticulum stressMammalian cellsTranscriptomic changesStress responseReticulum stressProtein levelsTranscriptsAbundanceCellsRelative contributionRecent reportsRegulationRecent workChallenging questions