Sarah Slavoff
Associate Professor Tenure of Chemistry and of Molecular Biophysics and BiochemistryCards
About
Research
Publications
Featured Publications
Mapping subcellular localizations of unannotated microproteins and alternative proteins with MicroID
Na Z, Dai X, Zheng SJ, Bryant CJ, Loh KH, Su H, Luo Y, Buhagiar AF, Cao X, Baserga SJ, Chen S, Slavoff SA. Mapping subcellular localizations of unannotated microproteins and alternative proteins with MicroID. Molecular Cell 2022, 82: 2900-2911.e7. PMID: 35905735, PMCID: PMC9662605, DOI: 10.1016/j.molcel.2022.06.035.Peer-Reviewed Original ResearchConceptsSubcellular localizationProximity biotinylationSmall open reading framesAlternative proteinsOpen reading frameHigh-throughput technologiesSubnuclear organellesCanonical proteinsRRNA transcriptionSubcellular compartmentsReading frameProteogenomic identificationProtein compositionAmino acidsMicroproteinsProteinBiotinylationLocalizationTurboIDTranscriptionOrganellesMouse modelPolypeptideNucleoliExpressionNascent alt-protein chemoproteomics reveals a pre-60S assembly checkpoint inhibitor
Cao X, Khitun A, Harold CM, Bryant CJ, Zheng SJ, Baserga SJ, Slavoff SA. Nascent alt-protein chemoproteomics reveals a pre-60S assembly checkpoint inhibitor. Nature Chemical Biology 2022, 18: 643-651. PMID: 35393574, PMCID: PMC9423127, DOI: 10.1038/s41589-022-01003-9.Peer-Reviewed Original ResearchConceptsRibosomal subunitDNA damage stressImportant cellular rolesGlobal protein synthesisN-terminal extensionCellular rolesCanonical proteinsHuman cellsProtein synthesisAlternative proteinsCell proliferationChemoproteomicsDamage stressSubunitsProteinAssemblyInhibitorsHypothesis generationMicroproteinsCytoplasmProliferationCellsExportDepletionAlt-RPL36 downregulates the PI3K-AKT-mTOR signaling pathway by interacting with TMEM24
Cao X, Khitun A, Luo Y, Na Z, Phoodokmai T, Sappakhaw K, Olatunji E, Uttamapinant C, Slavoff SA. Alt-RPL36 downregulates the PI3K-AKT-mTOR signaling pathway by interacting with TMEM24. Nature Communications 2021, 12: 508. PMID: 33479206, PMCID: PMC7820019, DOI: 10.1038/s41467-020-20841-6.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceBase SequenceBiological TransportCell MembraneDown-RegulationEndoplasmic ReticulumHEK293 CellsHumansMembrane ProteinsMutationPhosphatidylinositol 3-KinasesPhosphatidylinositol 4,5-DiphosphateProtein BindingProto-Oncogene Proteins c-aktRibosomal ProteinsSignal TransductionTOR Serine-Threonine KinasesConceptsPI3K-AktEndoplasmic reticulumMTOR signalingHuman gene functionAlternative open reading framesOpen reading framePI3K signalingDifferent molecular mechanismsCanonical proteinsGene functionCell sizeReading framePrecursor phosphatidylinositolPlasma membraneTMEM24Upstream regulatorMolecular mechanismsPhosphoserine residuesK signalingPoint mutationsSignalingPhosphatidylinositolProteinReticulumRPL36
2026
An expanded reference catalog of translated open reading frames for biomedical research
Chothani S, Ruiz-Orera J, Tierney J, Swirski M, Tjeldnes H, Kok L, Clauwaert J, Deutsch E, Alba M, Aspden J, Baranov P, Bazzini A, Bruford E, Brunet M, Cardon T, Carvunis A, Casola C, Choudhary J, Dean K, Faridi P, Fierro-Monti I, Fournier I, Frankish A, Gerstein M, Hubner N, Jiang Y, Kellis M, Martinez T, Menschaert G, Ni P, Orchard S, Roucou X, Rozowsky J, Salzet M, Siragusa M, Slavoff S, Ternette N, Vizcaino J, Wacholder A, Wu W, Xie Z, Yang Y, Moritz R, Valen E, Mudge J, van Heesch S, Prensner J, Rackham O. An expanded reference catalog of translated open reading frames for biomedical research. Nucleic Acids Research 2026, 54: gkag234. PMID: 41873765, PMCID: PMC13010147, DOI: 10.1093/nar/gkag234.Peer-Reviewed Original ResearchConceptsCanonical protein-coding genesReference genome annotationProtein-coding genesOpen reading frameEvidence of translationGenome annotationORF lengthReading frameDownstream analysisBiomedical researchNon-canonicalAnnotationORFData-driven frameworkTranslationCodonReproduced signalGenesTranslational evidenceCommunity benchmarking and evaluation of human unannotated microprotein detection by mass spectrometry based proteomics
Wacholder A, Deutsch E, Kok L, van Dinter J, Lee J, Wright J, Leblanc S, Jayatissa A, Jiang K, Arefiev I, Cao K, Bourassa F, Trifiro F, Bassani-Sternberg M, Baranov P, Bogaert A, Chothani S, Fierro-Monti I, Fijalkowska D, Gevaert K, Hubner N, Mudge J, Ruiz-Orera J, Schulz J, Vizcaíno J, Prensner J, Brunet M, Martinez T, Slavoff S, Roucou X, Choudhary J, van Heesch S, Moritz R, Carvunis A. Community benchmarking and evaluation of human unannotated microprotein detection by mass spectrometry based proteomics. Nature Communications 2026, 17: 1241. PMID: 41559053, PMCID: PMC12865046, DOI: 10.1038/s41467-025-68002-x.Peer-Reviewed Original ResearchConceptsShort open reading framesPeptide-spectrum matchesMass spectrometry (MS)-based proteomicsAnnotated coding sequenceOpen reading frameWhole cell lysatesUnannotated proteinsEnzymatic digestionReading frameMass spectrometryHuman proteinsManual curationCell lysatesProteinProtein detectionMicroproteinsPeptidomics datasetsProteomicsAnalysis workflowImmunopeptidomics studiesCommunity benchmarks
2025
Translon: a single term for translated regions
Świrski M, Tierney J, Albà M, Andreev D, Aspden J, Atkins J, Bassani-Sternberg M, Berry M, Biffo S, Boris-Lawrie K, Borodovsky M, Brierley I, Brook M, Brunet M, Bujnicki J, Caliskan N, Calviello L, Carvunis A, Cate J, Cenik C, Chang K, Chen Y, Chothani S, Choudhary J, Clark P, Clauwaert J, Cooley L, Dassi E, Dean K, Diaz J, Dieterich C, Dikstein R, Dinman J, Dmitriev S, Dontsova O, Dunham C, Eswarappa S, Farabaugh P, Faridi P, Fierro-Monti I, Firth A, Gatfield D, Gebauer F, Gelfand M, Gray N, Green R, Hill C, Hou Y, Hübner N, Ignatova Z, Ivanov P, Iwasaki S, Johnson R, Jomaa A, Jovanovic M, Jungreis I, Kellis M, Kieft J, Kochetov A, Koonin E, Korostelev A, Kufel J, Kulakovskiy I, Kurian L, Lafontaine D, Larsson O, Loughran G, Lukeš J, Mariotti M, Martens-Uzunova E, Martinez T, Matsumoto A, McManus J, Medenbach J, Melnikov S, Menschaert G, Merchante C, Mikl M, Miller W, Mühlemann O, Namy O, Nedialkova D, Nosek J, Orchard S, Ozretić P, Pertea M, Pervouchine D, Romão L, Ron D, Roucou X, Rubtsova M, Ruiz-Orera J, Saghatelian A, Salzberg S, Seale L, Seoighe C, Sergiev P, Shah P, Shirokikh N, Slavoff S, Sonenberg N, Stasevich T, Szczesny R, Tamm T, Tchórzewski M, Topisirovic I, Tremblay M, Tuller T, Ulitsky I, Valášek L, Van Damme P, Viero G, Vizcaino J, Vogel C, Wallace E, Weissman J, Westhof E, Whiffin N, Wilson D, Xie Z, Yewdell J, Yordanova M, Yu C, Yurchenko V, Zagrovic B, Valen E, Baranov P. Translon: a single term for translated regions. Nature Methods 2025, 22: 2002-2006. PMID: 40890551, DOI: 10.1038/s41592-025-02810-3.Peer-Reviewed Original ResearchLZTR1 is a melanoma oncogene that promotes invasion and suppresses apoptosis
Bacchiocchi A, Mak M, Khan Z, Gong X, Sznol M, Na Z, Su H, Chan L, Yan Q, Zhao D, Mortlock R, Knight J, Slavoff S, Halaban R. LZTR1 is a melanoma oncogene that promotes invasion and suppresses apoptosis. Oncogene 2025, 44: 3974-3984. PMID: 40885854, PMCID: PMC12500468, DOI: 10.1038/s41388-025-03538-2.Peer-Reviewed Original ResearchDegradation of ubiquitinated proteinsActin-related proteinsActin cytoskeleton organizationUbiquitin-proteasome systemSrc tyrosine kinaseAnchorage-independent growthNormal cell survivalCargo adapterActin organizationProximity biotinylationCytoskeleton organizationLC-MS/MS proteomicsLeucine zipperProteasome systemUbiquitinated proteinsCo-ImmunoprecipitationTargeting Pyk2Cell spreadingMelanoma cellsEnvironmental stressGrowth advantageMolecular characterizationCell migrationCell survivalLZTR1The ERVK3‑1 Microprotein Interacts with the HUSH Complex
Jayatissa A, Jaunbocus N, Erkalo B, Jiang K, Zheng S, Su H, Yan L, Choi J, Vaughan J, Bacchiocchi A, Na Z, Cao X, Halaban R, Saghatelian A, Craft J, Chen Y, Slavoff S. The ERVK3‑1 Microprotein Interacts with the HUSH Complex. Biochemistry 2025, 64: 3372-3381. PMID: 40699144, PMCID: PMC12339190, DOI: 10.1021/acs.biochem.5c00023.Peer-Reviewed Original ResearchConceptsHUSH complexTranscriptional repressionHuman endogenous retrovirusesIntron-less geneRegulation of target gene expressionEndogenous retrovirusesTarget gene expressionGenomic elementsHuman genomeTarget genesGene expressionHuman cellsMicroproteinsExogenous retrovirusesLociGenesRetrovirusesRetrotransposonsGenomeMolecular remnantsRepressionPPHLN1ComplexRegulationEukaryotic Microproteins
Jaunbocus N, Ebenki V, Su H, Slavoff S. Eukaryotic Microproteins. Annual Review Of Biochemistry 2025, 94: 1-28. PMID: 40245354, PMCID: PMC12207985, DOI: 10.1146/annurev-biochem-080124-012840.Peer-Reviewed Original Research
2021
Phosphorylation of a Human Microprotein Promotes Dissociation of Biomolecular Condensates
Na Z, Luo Y, Cui DS, Khitun A, Smelyansky S, Loria JP, Slavoff SA. Phosphorylation of a Human Microprotein Promotes Dissociation of Biomolecular Condensates. Journal Of The American Chemical Society 2021, 143: 12675-12687. PMID: 34346674, PMCID: PMC8564862, DOI: 10.1021/jacs.1c05386.Peer-Reviewed Original ResearchConceptsMembraneless organellesSmall open reading framesP-body dynamicsLiquid-liquid phase separationOpen reading frameGrowth factor signalingPresence of RNAEvolutionary conservationP-bodiesCellular processesCell divisionReading frameProteogenomic identificationFactor signalingMacromolecular complexesBiomolecular condensatesSecondary structureAmino acidsCell growthMicroproteinsPhosphorylationCell proliferationOrganellesBiophysical processesProliferation