Rag GTPases

Jenna L. Jewell; Kun Liang Guan

doi:10.1007/978-3-319-07761-1_12

Rag GTPases

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

The Rag GTPases appear to reside on the lysosome and link amino acid stimulation to mTOR complex 1 (mTORC1) activation. mTORC1 couples nutrient availability to cell growth. Dysregulation of mTORC1 is implicated in a number of human diseases, including cancer and diabetes. In response to amino acid availability the Rag GTPases are regulated by the Ragulator and GATOR complexes, which are a guanine nucleotide exchange factor (GEF) and GTPase activating protein (GAP), respectively. Here we review the current knowledge of Rag GTPases, with emphasis on amino acid-dependent regulation of mTORC1.

Original language	English (US)
Title of host publication	Ras Superfamily Small G Proteins
Subtitle of host publication	Biology and Mechanisms 2: Transport
Publisher	Springer International Publishing
Pages	277-292
Number of pages	16
ISBN (Electronic)	9783709118061
ISBN (Print)	3319077600, 9783709118054
DOIs	https://doi.org/10.1007/978-3-319-07761-1_12
State	Published - May 1 2014

Keywords

amino acids
Gator
lysosome
mTORC1
Rag GTPases
Ragulator
v-ATPase

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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10.1007/978-3-319-07761-1_12

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AB - The Rag GTPases appear to reside on the lysosome and link amino acid stimulation to mTOR complex 1 (mTORC1) activation. mTORC1 couples nutrient availability to cell growth. Dysregulation of mTORC1 is implicated in a number of human diseases, including cancer and diabetes. In response to amino acid availability the Rag GTPases are regulated by the Ragulator and GATOR complexes, which are a guanine nucleotide exchange factor (GEF) and GTPase activating protein (GAP), respectively. Here we review the current knowledge of Rag GTPases, with emphasis on amino acid-dependent regulation of mTORC1.

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Rag GTPases

Abstract

Keywords

ASJC Scopus subject areas

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