Biomedical datasets to: Functional proteomics identifies acinus L as a direct insulin- and amino acid-dependent mTORC1 substrate

  • Friedel Drepper (Data Manager)
  • Jennifer Jasmin Schwarz (Creator)
  • Heike Wiese (Creator)
  • Regine Charlotte Tölle (Creator)
  • Mostafa Zarei (Creator)
  • Jörn Dengjel (Creator)
  • Bettina Warscheid (Creator)
  • Kathrin Thedieck (Creator)



    The serine/threonine kinase mammalian target of rapamycin (mTOR) governs growth, metabolism, and aging in response to insulin and amino acids (aa), and is often activated in metabolic disorders and cancer. Much is known about the regulatory signaling network around mTOR, but surprisingly few direct mTOR substrates have been established to date. To tackle this gap in our knowledge, we took advantage of a combined quantitative phosphoproteomic and interactomic strategy. We analyzed the insulin- and aa-responsive phosphoproteome upon inhibition of the mTOR complex 1 (mTORC1) component raptor, and analyzed in parallel the interactome of endogenous mTOR. By overlaying these two datasets, we identified acinus L as a potential novel mTORC1 target. We confirmed acinus L as a direct mTORC1 substrate by co-immunoprecipitation and MS-enhanced kinase assays. Our study delineates a triple proteomics strategy of combined phosphoproteomics, interactomics, and MS-enhanced kinase assays for the de novo-identification of mTOR network components, and provides a rich source of potential novel mTOR interactors and targets for future investigation.
    Datum van beschikbaarheid28-apr-2015
    UitgeverEuropean Bioinformatics Institute (EMBL-EBI)

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