Mol. Cells 2013; 35(1): 1~6  DOI: 10.1007/s10059-013-2249-1
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
Received September 19, 2012; Revised December 4, 2012; Accepted December 4, 2012.; Published online December 26, 2012.
© The Korean Society for Molecular and Cellular Biology. All rights reserved.

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

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