mTORC1 phosphorylates the ULK1-mAtg13-FIP200 autophagy regulatory complex

Edmond Y Chan

Research output: Contribution to journalLiterature reviewpeer-review

174 Citations (Scopus)


High nutrient availability stimulates the mammalian target of rapamycin complex 1 (mTORC1) to coordinately activate anabolic processes, such as protein synthesis, while inhibiting the cellular catabolism of autophagy. Positive regulation of protein synthesis through the mTORC1 substrates p70 ribosomal S6 kinase (p70S6K) and eukaryotic initiation factor 4E binding protein 1 (4E-BP1) has been well characterized. The complementary inhibitory mechanism in which mTORC1 phosphorylates the autophagy regulatory complex containing unc-51-like kinase 1 (ULK1), the mammalian Atg13 protein, and focal adhesion kinase interacting protein of 200 kD (FIP200) has also been elucidated.
Original languageEnglish
Pages (from-to)pe51
JournalScience Signaling
Issue number84
Publication statusPublished - 18 Aug 2009


  • adaptor proteins
  • animals
  • autophagy
  • humans
  • intracellular signaling peptides
  • biological models
  • phosphorylation
  • protein-serine-threonine kinases
  • protein-tyrosine kinases
  • signal transduction
  • transcription factors


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