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 concentration
2020
SECAT: Quantifying Protein Complex Dynamics across Cell States by Network-Centric Analysis of SEC-SWATH-MS Profiles
Rosenberger G, Heusel M, Bludau I, Collins BC, Martelli C, Williams EG, Xue P, Liu Y, Aebersold R, Califano A. SECAT: Quantifying Protein Complex Dynamics across Cell States by Network-Centric Analysis of SEC-SWATH-MS Profiles. Cell Systems 2020, 11: 589-607.e8. PMID: 33333029, PMCID: PMC8034988, DOI: 10.1016/j.cels.2020.11.006.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsProtein complexesCell statesProtein complex dynamicsNative protein complexesMacromolecular complex formationPaper's transparent peer review processProtein interaction networksSEC-SWATHMultiple cell statesNetwork-centric analysisCellular processesInteraction networksMass spectrometric data analysisProteome OrganizationMolecular mechanismsRegulatory roleMass spectrometric analysisNetwork-based studyMultiplexed characterizationComplex formationSpectrometric data analysisSpectrometric analysisAlgorithmic toolkitState-specific changesA 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
2017
Proteotyping Gene Dosage Effects in Genetic Diseases
Liu Y, Aebersold R. Proteotyping Gene Dosage Effects in Genetic Diseases. The FASEB Journal 2017, 31 DOI: 10.1096/fasebj.31.1_supplement.926.3.Peer-Reviewed Original ResearchGene dosage imbalanceCopy number variationsProtein degradationDosage imbalanceGenetic diseasesSubstantial post-transcriptional regulationHeteromeric protein complexesDivergent expression levelsPost-transcriptional regulationCorresponding protein abundanceDNA copy number variationsComponents of pathwaysTurnover analysisPatient-derived induced pluripotent stem cellsInduced pluripotent stem cellsSWATH mass spectrometryPluripotent stem cellsGene dosage effectProtein turnover ratesPluripotent stateTranscript profilingSILAC experimentsProtein complexesTranslational regulationRNA-seq