Erratum to: Control of cell growth: Rag GTPases in activation of TORC1
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Cellular and Molecular Life Sciences
ERRATUM
Erratum to: Control of cell growth: Rag GTPases in activation of TORC1 Huirong Yang · Rui Gong · Yanhui Xu
Published online: 1 February 2013 © Springer Basel 2013
Erratum to: Cell Mol Life Sci DOI 10.1007/s00018-012-1195-y Unfortunately, the original publication of this paper contained errors in the presentation of Figs. 1 and 2. The corrected figures are given below.
The online version of the original article can be found under doi:10.1007/s00018-012-1195-y. H. Yang · R. Gong · Y. Xu (*) Cancer Institute, Shanghai Cancer Center, Fudan University, Shanghai 200032, People’s Republic of China e-mail: [email protected] H. Yang · R. Gong · Y. Xu Department of Oncology, Shanghai Medical College, Fudan University, Shanghai 200032, People’s Republic of China H. Yang · R. Gong · Y. Xu Institute of Biomedical Sciences, Fudan University, 130 Dong-An Road, Shanghai 200032, People’s Republic of China Y. Xu State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai 200433, People’s Republic of China
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Fig. 1 Rag GTPases in activation of mTORC1 signaling pathway in mammals. The mammalian target of rapamycin complex 1 (mTORC1) is a central regulator controlling cell growth through integrating signals from growth factors, cellular energy levels, stress, to amino acids. mTORC1 promotes mRNA translation by phosphorylation of S6K1 and 4E-BP1 and inhibits autophagy by phosphorylation of ATG13 and Ulk1. Growth factors stimulate mTORC1 through phosphorylation and inactivation of TSC1/2 complex. Akt phosphorylates TSC2 and inactivates the GAP activity of TSC1/2, leading to the activation of Rheb, which is essential for mTORC1 activation. AMPK is activated when cells are exposed to low energy (low ATP:ADP ratio). Stresses inhibit mTORC1 in part by reducing cellular ATP levels and leading to AMPK activation. Hypoxia also induces the expression of DNA damage response 1(REDD1), which activates TSC1/2 and inhibits mTORC1. Activated AMPK phosphorylates TSC2 and leads to activation of TSC1/2 GAP activity, Rheb inhibition, and mTORC1 inactivation. Rag GTPases play a central role in amino acid-induced mTORC1 activation. Rag GTPases form
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heterodimers and are localized on the late endosomal or lysosomal surface through the interaction with Ragulator complex (p18/MP1/ p14). The heterodimerization of Rag GTPases does not depend on amino acids, whereas the nucleotide loading status of Rag GTPases is regulated by amino acids through proteins as indicated. LRS is a leucine sensor and functions as a GAP for RagD GTPase to stimulate mTORC1 activity. Moreover, amino acid accumulation in lysosomal lumen promotes v-ATPase-mediated regulation of nucleotide loading on Rag GTPases. Active Rag GTPase heterodimers (RagA/ BGTP-RagC/DGDP) work together with Ragulator and v-ATPases to recruit mTORC1 to the lysosomal surface where Rheb is localized for mTORC1 activation. Adaptor protein p62 interacts with Rag GTPases to form a complex distinct f
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