Rags to riches: Amino acid sensing by the Rag GTPases in health and disease

Small GTPases. 2016 Oct;7(4):197-206. doi: 10.1080/21541248.2016.1218990. Epub 2016 Aug 31.

Abstract

The Rags represent a unique family of evolutionarily conserved, heterodimeric, lysosome-localized small GTPases that play an indispensible role in regulating cellular metabolism in response to various amino acid signaling mechanisms. Rapid progress in the field has begun to unveil a picture in which Rags act as central players in translating information regarding cellular amino acid levels by modulating their nucleotide binding status through an ensemble of support proteins localized in and around the lysosomes. By cooperating with other signaling pathways that converge on the lysosomes, Rags promote anabolic processes through positively affecting mTORC1 signaling in the presence of abundant amino acids. Conversely, Rag inactivation plays an indispensible role in switching cellular metabolism into a catabolic paradigm by promoting the activity of the master lysosomal/autophagic transcription factors TFEB and TFE3. Precise control of Rag signaling is necessary for cells to adapt to constantly changing cellular demands and emerging evidence has highlighted their importance in a wide variety of developmental and pathological conditions.

Keywords: Rags; TFE3; TFEB; autophagy; lysosomes; mTOR.

Publication types

  • Review

MeSH terms

  • Amino Acids / metabolism*
  • Basic Helix-Loop-Helix Leucine Zipper Transcription Factors / metabolism
  • Binding Sites
  • DNA-Binding Proteins / metabolism
  • Humans
  • Lysosomes / metabolism
  • Mechanistic Target of Rapamycin Complex 1
  • Monomeric GTP-Binding Proteins / chemistry
  • Monomeric GTP-Binding Proteins / genetics*
  • Monomeric GTP-Binding Proteins / metabolism*
  • Multiprotein Complexes / metabolism
  • Signal Transduction
  • TOR Serine-Threonine Kinases / metabolism

Substances

  • Amino Acids
  • Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
  • DNA-Binding Proteins
  • Multiprotein Complexes
  • Mechanistic Target of Rapamycin Complex 1
  • TOR Serine-Threonine Kinases
  • Monomeric GTP-Binding Proteins