Rag GTPases

Jenna L. Jewell, Kun Liang Guan

Research output: Chapter in Book/Report/Conference proceedingChapter

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 languageEnglish (US)
Title of host publicationRas Superfamily Small G Proteins
Subtitle of host publicationBiology and Mechanisms 2: Transport
PublisherSpringer International Publishing
Pages277-292
Number of pages16
ISBN (Electronic)9783709118061
ISBN (Print)3319077600, 9783709118054
DOIs
StatePublished - May 1 2014

Fingerprint

GTP Phosphohydrolases
Amino Acids
Availability
GTPase-Activating Proteins
Guanine Nucleotide Exchange Factors
Cell growth
Medical problems
Lysosomes
Nutrients
Chemical activation
Food
Growth
Neoplasms

Keywords

  • amino acids
  • Gator
  • lysosome
  • mTORC1
  • Rag GTPases
  • Ragulator
  • v-ATPase

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Jewell, J. L., & Guan, K. L. (2014). Rag GTPases. In Ras Superfamily Small G Proteins: Biology and Mechanisms 2: Transport (pp. 277-292). Springer International Publishing. https://doi.org/10.1007/978-3-319-07761-1_12

Rag GTPases. / Jewell, Jenna L.; Guan, Kun Liang.

Ras Superfamily Small G Proteins: Biology and Mechanisms 2: Transport. Springer International Publishing, 2014. p. 277-292.

Research output: Chapter in Book/Report/Conference proceedingChapter

Jewell, JL & Guan, KL 2014, Rag GTPases. in Ras Superfamily Small G Proteins: Biology and Mechanisms 2: Transport. Springer International Publishing, pp. 277-292. https://doi.org/10.1007/978-3-319-07761-1_12
Jewell JL, Guan KL. Rag GTPases. In Ras Superfamily Small G Proteins: Biology and Mechanisms 2: Transport. Springer International Publishing. 2014. p. 277-292 https://doi.org/10.1007/978-3-319-07761-1_12
Jewell, Jenna L. ; Guan, Kun Liang. / Rag GTPases. Ras Superfamily Small G Proteins: Biology and Mechanisms 2: Transport. Springer International Publishing, 2014. pp. 277-292
@inbook{14d6535a10a943f5b5dc374844c8b664,
title = "Rag GTPases",
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.",
keywords = "amino acids, Gator, lysosome, mTORC1, Rag GTPases, Ragulator, v-ATPase",
author = "Jewell, {Jenna L.} and Guan, {Kun Liang}",
year = "2014",
month = "5",
day = "1",
doi = "10.1007/978-3-319-07761-1_12",
language = "English (US)",
isbn = "3319077600",
pages = "277--292",
booktitle = "Ras Superfamily Small G Proteins",
publisher = "Springer International Publishing",

}

TY - CHAP

T1 - Rag GTPases

AU - Jewell, Jenna L.

AU - Guan, Kun Liang

PY - 2014/5/1

Y1 - 2014/5/1

N2 - 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.

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.

KW - amino acids

KW - Gator

KW - lysosome

KW - mTORC1

KW - Rag GTPases

KW - Ragulator

KW - v-ATPase

UR - http://www.scopus.com/inward/record.url?scp=84930359291&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84930359291&partnerID=8YFLogxK

U2 - 10.1007/978-3-319-07761-1_12

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

M3 - Chapter

AN - SCOPUS:84930359291

SN - 3319077600

SN - 9783709118054

SP - 277

EP - 292

BT - Ras Superfamily Small G Proteins

PB - Springer International Publishing

ER -