Chan, Edmond Y (2009) mTORC1 phosphorylates the ULK1-mAtg13-FIP200 autophagy regulatory complex. Science signaling, 2 (84). pe51.Full text not available in this repository. (Request a copy from the Strathclyde author)
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.
|Keywords:||adaptor proteins, animals, autophagy, humans, intracellular signaling peptides , biological models, phosphorylation, protein-serine-threonine kinases, protein-tyrosine kinases, signal transduction, transcription factors, Therapeutics. Pharmacology, Medicine(all)|
|Subjects:||Medicine > Therapeutics. Pharmacology|
|Department:||Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences|
|Depositing user:||Pure Administrator|
|Date Deposited:||10 Aug 2011 12:54|
|Last modified:||24 Mar 2017 06:17|