mTORC1 Phosphorylates the ULK1-mAtg13-FIP200 Autophagy Regulatory Complex

Edmond Y. Chan^*

Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, 27 Taylor Street, Glasgow G4 0NR, UK.

Abstract: 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.

* Corresponding author. E-mail: edmond.chan{at}strath.ac.uk

The editors suggest the following Related Resources on Science sites:

In Science Signaling

EDITORIAL GUIDES
Cell Biology
Focus Issue: Demystifying mTOR Signaling

Nancy R. Gough (21 April 2009)
Sci. Signal. 2 (67), eg5. [DOI: 10.1126/scisignal.267eg5]
 |  Abstract »  |  Full Text »  |  PDF »

EDITORS' CHOICE
Cell Biology
Doing the Glutamine Two-Step

Elizabeth M. Adler (10 February 2009)
Sci. Signal. 2 (57), ec48. [DOI: 10.1126/scisignal.257ec48]
 |  Abstract »

EDITORS' CHOICE
CELL BIOLOGY
Autophagy and Growth

(17 August 2004)
Sci. STKE 2004 (246), tw291. [DOI: 10.1126/stke.2462004tw291]
 |  Abstract »