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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Ras-related GTP binding C

RRAGC is a monomeric guanine nucleotide-binding protein, or G protein. By binding GTP or GDP, small G proteins act as molecular switches in numerous cell processes and signaling pathways.[supplied by OMIM, Apr 2004] (from NCBI)
Top mentioned proteins: mTORC1, ACID, mTOR, RagB, Rheb
Papers on RagC
RRAGC Mutations Activate mTORC1 Signaling in Follicular Lymphoma.
In Cancer Discov, Feb 2016
UNASSIGNED: RRAGC mutations in follicular lymphoma activate mTORC1, even during amino acid depletion.
Recurrent mTORC1-activating RRAGC mutations in follicular lymphoma.
Fitzgibbon et al., Cambridge, United States. In Nat Genet, Jan 2016
Using a combination of discovery exome and extended targeted sequencing, we identified recurrent somatic mutations in RRAGC uniquely enriched in patients with follicular lymphoma (17%).
Amino Acid-Induced Activation of mTORC1 in Rat Liver Is Attenuated by Short-Term Consumption of a High-Fat Diet.
Jefferson et al., State College, United States. In J Nutr, Nov 2015
Livers were collected and analyzed for mTORC1 signaling [assessed by changes in phosphorylation of 70-kDa ribosomal protein S6 kinase 1 (p70S6K1) and eukaryotic initiation factor 4E binding protein 1 (4E-BP1)] and potential regulatory mechanisms, including changes in the association of Ras-related GTP binding (Rag) A and RagC with mechanistic target of rapamycin (mTOR) and expression of Sestrin1, Sestrin2, and Sestrin3.
Cystinosin is a Component of the Vacuolar H+-ATPase-Ragulator-Rag Complex Controlling Mammalian Target of Rapamycin Complex 1 Signaling.
Antignac et al., Paris, France. In J Am Soc Nephrol, Nov 2015
By coimmunoprecipitation experiments and mass spectrometry, we found cystinosin interacts with almost all components of vacuolar H(+)-ATPase and the Ragulator complex and with the small GTPases Ras-related GTP-binding protein A (RagA) and RagC.
Amino Acids Stimulate TORC1 through Lst4-Lst7, a GTPase-Activating Protein Complex for the Rag Family GTPase Gtr2.
De Virgilio et al., Fribourg, Switzerland. In Cell Rep, Nov 2015
Rag GTPases assemble into heterodimeric complexes consisting of RagA or RagB and RagC or RagD in higher eukaryotes, or Gtr1 and Gtr2 in yeast, to relay amino acid signals toward the growth-regulating target of rapamycin complex 1 (TORC1).
Sepsis-induced changes in amino acid transporters and leucine signaling via mTOR in skeletal muscle.
Lang et al., State College, United States. In Amino Acids, 2014
The binding of mTOR, PRAS40 and RagC to raptor did not differ for control and septic muscle in the basal condition; however, the Leu-induced decrease in PRAS40·raptor and increase in RagC·raptor seen in control muscle was absent in sepsis.
Sestrins inhibit mTORC1 kinase activation through the GATOR complex.
Budanov et al., In Cell Rep, 2014
mTORC1 is activated by Rag GTPases, working as RagA:RagB and RagC:RagD heterodimers.
The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1.
Sabatini et al., Cambridge, United States. In Cell Rep, 2014
A key input is amino acids, which act through the heterodimeric Rag GTPases (RagA or RagB bound to RagC or RagD) in order to promote the translocation of mTORC1 to the lysosomal surface, its site of activation.
Sestrins function as guanine nucleotide dissociation inhibitors for Rag GTPases to control mTORC1 signaling.
Li et al., New York City, United States. In Cell, 2014
Here, we show that Sestrins bind to the heterodimeric RagA/B-RagC/D GTPases, and function as guanine nucleotide dissociation inhibitors (GDIs) for RagA/B.
Genetic analysis of Leishmania donovani tropism using a naturally attenuated cutaneous strain.
Matlashewski et al., Montréal, Canada. In Plos Pathog, 2014
This is illustrated through the observations within showing that a decreased copy number of the A2 gene family and a mutation in the ras-like RagC GTPase enzyme in the mTOR pathway contribute to the attenuation of the CL-SL strain in visceral infection.
Amino acids activate mammalian target of rapamycin (mTOR) complex 1 without changing Rag GTPase guanyl nucleotide charging.
Avruch et al., Boston, United States. In J Biol Chem, 2014
Such a mutation in RagA or RagB inhibits, whereas in RagC or RagD it enhances, Rag heterodimer binding to mTORC1.
Differential activation of mTOR complex 1 signaling in human brain with mild to severe Alzheimer's disease.
Jin et al., Beijing, China. In J Alzheimers Dis, 2013
Autopsy brain hippocampal tissues were obtained from controls and patients with AD and Western blots were performed using antibodies against mTOR signaling molecules and RagC, an upstream component of mTOR complex 1 (mTORC1) signaling.
The putative HORMA domain protein Atg101 dimerizes and is required for starvation-induced and selective autophagy in Drosophila.
Juhász et al., Budapest, Hungary. In Biomed Res Int, 2013
Atg101 interacts with ref(2)P as well, similar to Atg13, Atg8a, Atg16, Atg18, Keap1, and RagC, a known regulator of Tor kinase which coordinates cell growth and autophagy.
The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1.
Sabatini et al., Cambridge, United States. In Mol Cell, 2013
The Rags are unusual GTPases in that they function as obligate heterodimers, which consist of RagA or B bound to RagC or D. While the loading of RagA/B with GTP initiates amino acid signaling to mTORC1, the role of RagC/D is unknown.
Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1.
Sabatini et al., Cambridge, United States. In Cell, 2012
The heterodimeric RagA/B-RagC/D GTPases, the Ragulator complex that tethers the Rags to the lysosome, and the v-ATPase form a signaling system that is necessary for amino acid sensing by mTORC1.
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