Abstract: Target of rapamycin (TOR) is a central regulator of cell growth conserved from yeast to mammals. TOR is a member of the phosphoinositide-3-kinase-related protein kinase family, which includes ATM, ATR, DNA-PK, and TOR [1]. In both yeast and human, TOR forms two distinct structural and functional complexes, TORCs. The mammalian TORC1 (mTORC1) consists of mTOR, raptor, mLST8, and PRAS40 2, 3, 4, 5, 6 while mTORC2 consists of mTOR, rictor, sin1, and mLTS8 7, 8, 9, 10. mTORC1 (at least part of the mTORC1 function) is potently inhibited by rapamycin while mTORC2 is not directly inhibited by rapamycin [11]. Characterized substrates of mTORC1 include the ribosomal S6 kinase (S6K), eukaryote initiation factor 4E binding protein (4EBP1) [12], and the autophagy regulatory kinase ATG1 13, 14, 15. Therefore, mTORC1 plays a critical role in translation, cell growth, and autophagy. In contrast, mTORC2 is required for phosphorylation of AKT [16], SGK [17], and conventional PKC 18, 19, suggesting that the two TOR complexes have different physiological functions. This chapter will mainly discuss the regulation of mTORC1 by amino acids and the role of Rag GTPases in nutrient response.
Publication Year: 2004
Publication Date: 2004-09-01
Language: en
Type: article
Indexed In: ['crossref']
Access and Citation
AI Researcher Chatbot
Get quick answers to your questions about the article from our AI researcher chatbot