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Mol. Cells 2013; 35(1): 1-6

Published online January 31, 2013

https://doi.org/10.1007/s10059-013-2249-1

© The Korean Society for Molecular and Cellular Biology

dRAGging Amino Acid-mTORC1 Signaling by SH3BP4

Young-Mi Kim1, and Do-Hyung Kim1,2,*

1Department of Biochemistry, Molecular Biology and Biophysics, 2Masonic Cancer Center, University of Minnesota, Minneapolis, MN 55455, USA

Correspondence to : *Correspondence: dhkim@umn.edu

Received: September 19, 2012; Revised: December 4, 2012; Accepted: December 4, 2012

Abstract

Mammalian target of rapamycin complex 1 (mTORC1) is a master regulator of cell growth and autophagy. Its activity is regulated by the availability of amino acids and growth factors. The activation of mTORC1 by growth factors, such as insulin and insulin-like growth factor-1 (IGF-1), is mediated by tuberous sclerosis complex (TSC) 1 and 2 and Rheb GTPase. Relative to the growth factor-regulated mTORC1 pathway, the evolutionarily ancient amino acidmTORC1 pathway remains not yet clearly defined. The amino acid-mTORC1 pathway is mediated by Rag GTPase heterodimers. Several binding proteins of Rag GTPases were discovered in recent studies. Here, we discuss the functions and mechanisms of the newly-identified binders of Rag GTPases. In particular, this review focuses on SH3 binding protein 4 (SH3BP4), the protein recently identifed as a negative regulator of Rag GTPases.

Keywords mTOR, mTORC1, Rag GTPases, SH3BP4

Article

Minireview

Mol. Cells 2013; 35(1): 1-6

Published online January 31, 2013 https://doi.org/10.1007/s10059-013-2249-1

Copyright © The Korean Society for Molecular and Cellular Biology.

dRAGging Amino Acid-mTORC1 Signaling by SH3BP4

Young-Mi Kim1, and Do-Hyung Kim1,2,*

1Department of Biochemistry, Molecular Biology and Biophysics, 2Masonic Cancer Center, University of Minnesota, Minneapolis, MN 55455, USA

Correspondence to:*Correspondence: dhkim@umn.edu

Received: September 19, 2012; Revised: December 4, 2012; Accepted: December 4, 2012

Abstract

Mammalian target of rapamycin complex 1 (mTORC1) is a master regulator of cell growth and autophagy. Its activity is regulated by the availability of amino acids and growth factors. The activation of mTORC1 by growth factors, such as insulin and insulin-like growth factor-1 (IGF-1), is mediated by tuberous sclerosis complex (TSC) 1 and 2 and Rheb GTPase. Relative to the growth factor-regulated mTORC1 pathway, the evolutionarily ancient amino acidmTORC1 pathway remains not yet clearly defined. The amino acid-mTORC1 pathway is mediated by Rag GTPase heterodimers. Several binding proteins of Rag GTPases were discovered in recent studies. Here, we discuss the functions and mechanisms of the newly-identified binders of Rag GTPases. In particular, this review focuses on SH3 binding protein 4 (SH3BP4), the protein recently identifed as a negative regulator of Rag GTPases.

Keywords: mTOR, mTORC1, Rag GTPases, SH3BP4

Mol. Cells
Sep 30, 2022 Vol.45 No.9, pp. 603~672
COVER PICTURE
The Target of Rapamycin Complex (TORC) is a central regulatory hub in eukaryotes, which is well conserved in diverse plant species, including tomato (Solanum lycopersicum). Inhibition of TORC genes (SlTOR, SlLST8, and SlRAPTOR) by VIGS (virus-induced gene silencing) results in early fruit ripening in tomato. The red/ orange tomatoes are early-ripened TORC-silenced fruits, while the green tomato is a control fruit. Top, left, control fruit (TRV2-myc); top, right, TRV2-SlLST8; bottom, left, TRV2-SlTOR; bottom, right, TRV2-SlRAPTOR(Choi et al., pp. 660-672).

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