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mTORC1 as the main gateway to autophagy

Lookup NU author(s): Dr Yoana Rabanal Ruiz, Gisela Otten, Dr Viktor Korolchuk



This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


© 2017 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society. Cells and organisms must coordinate their metabolic activity with changes in their environment to ensure their growth only when conditions are favourable. In order to maintain cellular homoeostasis, a tight regulation between the synthesis and degradation of cellular components is essential. At the epicentre of the cellular nutrient sensing is the mechanistic target of rapamycin complex 1 (mTORC1) which connects environmental cues, including nutrient and growth factor availability as well as stress, to metabolic processes in order to preserve cellular homoeostasis. Under nutrient-rich conditions mTORC1 promotes cell growth by stimulating biosynthetic pathways, including synthesis of proteins, lipids and nucleotides, and by inhibiting cellular catabolism through repression of the autophagic pathway. Its close signalling interplay with the energy sensor AMP-Activated protein kinase (AMPK) dictates whether the cell actively favours anabolic or catabolic processes. Underlining the role of mTORC1 in the coordination of cellular metabolism, its deregulation is linked to numerous human diseases ranging from metabolic disorders to many cancers. Although mTORC1 can be modulated by a number of different inputs, amino acids represent primordial cues that cannot be compensated for by any other stimuli. The understanding of how amino acids signal to mTORC1 has increased considerably in the last years; however this area of research remains a hot topic in biomedical sciences. The current ideas and models proposed to explain the interrelationship between amino acid sensing, mTORC1 signalling and autophagy is the subject of the present review.

Publication metadata

Author(s): Rabanal-Ruiz Y, Otten EG, Korolchuk VI

Publication type: Review

Publication status: Published

Journal: Essays in Biochemistry

Year: 2017

Volume: 61

Issue: 6

Pages: 565-584

Print publication date: 12/12/2017

Online publication date: 12/12/2017

Acceptance date: 02/04/2016

ISSN (print): 0071-1365

ISSN (electronic): 1744-1358

Publisher: Portland Press Ltd


DOI: 10.1042/EBC20170027