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DTSTART;TZID=Europe/Stockholm:20221215T160000
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DTSTAMP:20260424T060008
CREATED:20221212T155650Z
LAST-MODIFIED:20221212T155652Z
UID:146305-1671120000-1671123600@www.scilifelab.se
SUMMARY:Functional analysis of human protein phosphorylation sites
DESCRIPTION:Matthias Selbach  \n\n\n\nPhosphoproteomics routinely quantifies changes in the levels of thousands of phosphorylation sites\, but functional analysis of such data remains a major challenge. I will present three different ways to characterise the function of human phosphorylation sites. First\, I will show how data from in vitro kinase assays can be used to predict kinase activity in phosphoproteomic datasets. Second\, I will show quantitative affinity purification experiments with synthetic phosphopeptides can help to assess their cellular function. Finally\, I will outline how quantitative RNA-interactome capture (qRIC) can quantify the fraction of cellular RNA-binding proteins that are pulled down with polyadenylated mRNAs. Combining qRIC with phosphoproteomics allows us to systematically compare pull-down efficiencies of phosphorylated and non-phosphorylated forms of RBPs. Using qRIC\, we identify over hundred phosphorylation sites with regulatory potential\, including known regulatory sites. Follow-up experiments on the cardiac splicing regulator RBM20 revealed that multiple phosphorylation sites in the C-terminal disordered region affect nucleo-cytoplasmic localisation\, association with cytosolic RNA granules and alternative splicing.      \n\n\n\nSelected publications\n\n\n\n\nVieira-Vieira\, CH\, Dauksaite\, V.\, Sporbert\, A.\, Gotthardt\, M. and Selbach M. (2022) Proteome-wide quantitative RNA-interactome capture identifies phosphorylation sites with regulatory potential in RBM20. Mol Cell 82\, 2069-2083.\n\n\n\nMeyer\, K.\, Kirchner\, M.\, Uyar\, B.\, Cheng\, J.Y.\, Russo\, G.\, …\, and Selbach\, M. (2018). Mutations in Disordered Regions Can Cause Disease by Creating Dileucine Motifs. Cell 175\, 239-253.\n\n\n\nImami\, K.\, Milek\, M.\, Bogdanow\, B.\, Yasuda\, T.\, Kastelic\, N.\, …\, and Selbach\, M. (2018). Mol Cell. Phosphorylation of the Ribosomal Protein RPL12/uL11 Affects Translation during Mitosis. Mol Cell 72\,\n\n\n\nZauber\, H.\, Kirchner\, M.\, and Selbach\, M. (2018). Picky: a simple online PRM and SRM method designer for targeted proteomics. Nat Methods 15\, 156-157.\n\n\n\nMcShane\, E.\, Sin\, C.\, Zauber\, H\, Wells JN\, Donnelly N\, …\, and Selbach M. (2016). Kinetic analysis of protein stability reveals age-dependent degradation. Cell 167\, 803-815.\n\n\n\nSchwanhausser\, B.\, Busse\, D.\, Li\, N.\, Dittmar\, G.\, Schuchhardt\, J.\, Wolf\, J.\, Chen\, W.\, and Selbach\, M. (2011). Global quantification of mammalian gene expression control. Nature 473\, 337-342.
URL:https://www.scilifelab.se/event/functional-analysis-of-human-protein-phosphorylation-sites/
LOCATION:Air&Fire\, SciLifeLab Stockholm\, Tomtebodavägen 23A\, Solna\, Sweden
CATEGORIES:Event
ORGANIZER;CN="Janne Lehti%C3%B6":MAILTO:janne.lehtio@scilifelab.se
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