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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 B

Ras-homologous GTPases constitute a large family of signal transducers that alternate between an activated, GTP-binding state and an inactivated, GDP-binding state. These proteins represent cellular switches that are operated by GTP-exchange factors and factors that stimulate their intrinsic GTPase activity. All GTPases of the Ras superfamily have in common the presence of six conserved motifs involved in GTP/GDP binding, three of which are phosphate-/magnesium-binding sites (PM1-PM3) and three of which are guanine nucleotide-binding sites (G1-G3). Transcript variants encoding distinct isoforms have been identified. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: mTORC1, ACID, mTOR, RagC, HAD
Papers on RagB
Pharmacological inhibition of fatty-acid oxidation synergistically enhances the effect of l-asparaginase in childhood ALL cells.
Starkova et al., Praha, Czech Republic. In Leukemia, Jan 2016
FAO, together with the decrease in protein translation and pyrimidine synthesis, was positively regulated through inhibition of the RagB-mTORC1 pathway, whereas the effect on glycolysis was RagB-mTORC1 independent.
Structure of RagB, a major immunodominant outer-membrane surface receptor antigen of Porphyromonas gingivalis.
Gomis-RĂ¼th et al., Barcelona, Spain. In Mol Oral Microbiol, Nov 2015
UNASSIGNED: Porphyromonas gingivalis is the main causing agent of periodontitis.
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).
V-ATPase: a master effector of E2F1-mediated lysosomal trafficking, mTORC1 activation and autophagy.
Tauler et al., Barcelona, Spain. In Oncotarget, Oct 2015
Immunoprecipitation experiments demonstrate that E2F1 induces the recruitment of v-ATPase to lysosomal RagB GTPase, suggesting that E2F1 regulates v-ATPase activity by enhancing the association of V0 and V1 v-ATPase complex.
Porphyromonas gingivalis B cell Antigen Epitope Vaccine, pIRES-ragB'-mGITRL, Promoted RagB-Specific Antibody Production and Tfh Cells Expansion.
Su et al., Zhenjiang, China. In Scand J Immunol, Jun 2015
The outer membrane protein RagB is one of the major virulence factors of Porphyromonas gingivalis (P.
Dichotomy of Genetic Abnormalities in PEComas With Therapeutic Implications.
Antonescu et al., New York City, United States. In Am J Surg Pathol, Jun 2015
In addition, novel RAD51B gene rearrangements were identified in 3 (8%) uterine PEComas, which showed a complex fusion pattern and were fused to RRAGB/OPHN1 genes in 2 cases.
Porphyromonas gingivalis RagB is a proinflammatory signal transducer and activator of transcription 4 agonist.
Scott et al., Louisville, United States. In Mol Oral Microbiol, Jun 2015
The 55-kDa immunodominant RagB outer membrane protein of Porphyromonas gingivalis, a keystone periodontal pathogen, has been proposed to facilitate nutrient transport.
Metabolism. Differential regulation of mTORC1 by leucine and glutamine.
Guan et al., San Diego, United States. In Science, Feb 2015
Glutamine promoted mTORC1 translocation to the lysosome in RagA and RagB knockout cells and required the v-ATPase but not the Ragulator.
Sestrin2 inhibits mTORC1 through modulation of GATOR complexes.
Lee et al., Ann Arbor, United States. In Sci Rep, 2014
GATORs are recently identified protein complexes that regulate the activity of RagB, a small GTPase essential for mTORC1 activation.
Metaproteomics reveals the major microbial players and their biogeochemical functions in a productive coastal system in the northern South China Sea.
Xie et al., In Environ Microbiol Rep, 2014
Expression of proteorhodopsin and RagB/SusD from Flavobacteria facilitates their attachment and growth on algal-derived organic matter.
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.
Reassessment of the role of TSC, mTORC1 and microRNAs in amino acids-meditated translational control of TOP mRNAs.
Meyuhas et al., Jerusalem, Israel. In Plos One, 2013
The signaling of amino acids to TOP mRNAs involves RagB, as overexpression of active RagB derepressed the translation of these mRNAs in amino acid-starved cells.
A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1.
Sabatini et al., Cambridge, United States. In Science, 2013
GATOR1 has GTPase-activating protein (GAP) activity for RagA and RagB, and its components are mutated in human cancer.
Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1.
Sabatini et al., Cambridge, United States. In Cell, 2012
Amino acids stimulate the binding of guanosine triphosphate to RagA and RagB but the factors that regulate Rag nucleotide loading are unknown.
Glutaminolysis activates Rag-mTORC1 signaling.
Hall et al., Basel, Switzerland. In Mol Cell, 2012
Inhibition of glutaminolysis prevents GTP loading of RagB and lysosomal translocation and subsequent activation of mTORC1.
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