Affinage

RRAGB

Ras-related GTP-binding protein B · UniProt Q5VZM2

Round 2 corrected
Length
374 aa
Mass
43.2 kDa
Annotated
2026-04-28
44 papers in source corpus 19 papers cited in narrative 18 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RRAGB (RagB) is a Ras-family small GTPase that forms obligate heterodimers with RagC or RagD and serves as a central mediator of amino acid signaling to mTORC1, coupling nutrient availability to cell growth (PMID:18497260, PMID:11073942). In response to amino acids, RagB is loaded with GTP through the guanine nucleotide exchange activity of the lysosome-anchored Ragulator complex, while leucyl-tRNA synthetase and GATOR1 act as GAPs, and Sestrins function as GDIs to negatively regulate its activation; the active RagB–RagC/D heterodimer recruits mTORC1 to lysosomal membranes where it is activated by Rheb (PMID:22980980, PMID:22424946, PMID:23723238, PMID:25259925, PMID:20381137). Upstream nutrient inputs including arginine sensing via the lysosomal transporter SLC38A9, glutaminolysis-derived α-ketoglutarate, folliculin (FLCN), p62/SQSTM1, and the SZT2-organized GATOR complex converge on the RagB nucleotide cycle to tune mTORC1 activation (PMID:25567906, PMID:22749528, PMID:24081491, PMID:21981924, PMID:28199315). RRAGB overexpression in glioblastoma cells suppresses proliferation through inhibition of PI3K/AKT signaling, and HIF1A transcriptionally upregulates RRAGB, indicating additional regulatory and context-dependent roles in cancer biology (PMID:37517217, PMID:35739524).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2000 High

    Identification of RagC/D as obligate heterodimeric partners of RagA/B established the fundamental Rag GTPase architecture, resolving how these atypical small GTPases are organized.

    Evidence Yeast two-hybrid, GST pulldown, and GTP/GDP binding assays in mammalian cells

    PMID:11073942

    Open questions at the time
    • No upstream regulation or downstream effector identified at this stage
    • Functional relevance of heterodimer to signaling pathways unknown
  2. 2008 High

    Linking RagB GTP loading to amino acid-dependent mTORC1 activation and lysosomal translocation revealed the core physiological function of the Rag GTPases, answering what signal they relay and to whom.

    Evidence Co-IP of Rag–Raptor, constitutively active/dominant-negative RagB mutants, mTOR lysosomal localization imaging

    PMID:18497260

    Open questions at the time
    • Mechanism anchoring Rag GTPases to lysosomes unknown
    • Identity of the RagB GEF and GAP unresolved
  3. 2010 High

    Discovery that the Ragulator complex tethers Rag GTPases to lysosomes and that constitutive lysosomal targeting of mTORC1 bypasses Rag/Ragulator dependence established lysosomal recruitment as the rate-limiting step in amino acid sensing.

    Evidence Co-IP, lysosomal localization imaging, constitutively lysosome-targeted mTORC1 epistasis

    PMID:20381137

    Open questions at the time
    • Whether Ragulator has catalytic activity toward Rag GTPases undetermined
    • Upstream amino acid sensors unidentified
  4. 2011 High

    Identification of p62/SQSTM1 as an amino acid-dependent binding partner of Rag GTPases that stabilizes the active heterodimer and promotes mTORC1 lysosomal recruitment added a regulatory scaffold component to the pathway.

    Evidence Co-IP, co-localization imaging, amino acid-dependent interaction assays, knockdown with mTORC1 readouts

    PMID:21981924

    Open questions at the time
    • Precise mechanism by which p62 stabilizes the active Rag configuration unclear
    • Relationship to p62's role in autophagy not dissected
  5. 2012 High

    Three concurrent discoveries defined the enzymology governing RagB nucleotide state: Ragulator as the GEF, leucyl-tRNA synthetase as a leucine-sensing GAP, and glutaminolysis/α-ketoglutarate as an upstream signal promoting RagB GTP loading.

    Evidence In vitro GEF assay for Ragulator, in vitro GAP assay for LRS with leucine-binding mutagenesis, RagB nucleotide loading assays with glutaminolysis inhibition and constitutively active Rag rescue

    PMID:22424946 PMID:22749528 PMID:22980980

    Open questions at the time
    • Structural basis of Ragulator GEF activity unresolved
    • LRS GAP activity questioned by later studies regarding specificity for RagD vs RagB
    • How α-ketoglutarate mechanistically influences RagB GTP loading unclear
  6. 2013 High

    Identification of GATOR1 as a RagA/B GAP and FLCN as a direct RagA/B-binding protein defined key negative and positive regulators converging on Rag nucleotide cycling, and linked GATOR1 loss-of-function to cancer.

    Evidence In vitro GAP assay for GATOR1 on RagA/B, cancer cell line GATOR1 knockdown; Co-IP of FLCN with RagA/B, FLCN knockout epistasis

    PMID:23723238 PMID:24081491

    Open questions at the time
    • Whether FLCN has direct catalytic activity toward Rag GTPases unresolved at this point
    • Structural basis of GATOR1 GAP mechanism unknown
  7. 2014 High

    Demonstration that Sestrins act as GDIs for RagA/B revealed a distinct inhibitory mechanism—blocking nucleotide exchange rather than stimulating GTP hydrolysis—adding a new regulatory modality to the pathway.

    Evidence In vitro GDI assay, GDI motif mutagenesis, cell-permeable peptide inhibition, mouse knockout

    PMID:25259925

    Open questions at the time
    • How Sestrin GDI activity is itself regulated by stress signals incompletely understood
    • Whether Sestrins have additional Rag-independent functions in mTORC1 regulation unclear
  8. 2015 High

    SLC38A9 was identified as a lysosomal arginine sensor upstream of Rag GTPases, providing the first mechanistic link between a specific amino acid transporter and the Rag-mTORC1 pathway.

    Evidence Co-IP of SLC38A9 with Rag GTPases and Ragulator, arginine transport assay, loss-of-function and gain-of-function epistasis

    PMID:25561175 PMID:25567906

    Open questions at the time
    • How SLC38A9 mechanistically alters Rag nucleotide state not determined
    • Whether SLC38A9 senses luminal arginine directly or indirectly debated
  9. 2017 High

    Discovery that SZT2 organizes GATOR1/GATOR2 into the SOG complex at lysosomes explained how GATOR-mediated Rag regulation is spatially coordinated, resolving how nutrient-insensitive mTORC1 signaling arises from SZT2 deficiency.

    Evidence Co-IP, lysosomal localization, genetic knockout mouse, GATOR1/2 epistasis

    PMID:28199315

    Open questions at the time
    • Whether SZT2 has additional scaffolding roles beyond GATOR complex organization unknown
    • Structural basis of SOG complex assembly unresolved
  10. 2018 Medium

    TRIM37 was shown to enhance the mTOR–RRAGB interaction and promote mTOR lysosomal localization, identifying a new positive regulator that also connects Rag-mTORC1 signaling to TFEB-dependent lysosome biogenesis.

    Evidence Co-IP of TRIM37 with mTOR and RRAGB, lysosomal localization imaging, TFEB phosphorylation assays

    PMID:29940807

    Open questions at the time
    • Whether TRIM37's E3 ligase activity is required for its effect on RRAGB not established
    • Single-lab finding awaiting independent replication
  11. 2022 Medium

    Two studies expanded the regulatory landscape: NUFIP2/galectin-8 were found to inactivate the Rag complex at damaged lysosomes, and circEXOC6B was shown to directly bind RRAGB to inhibit heterodimer formation, while HIF1A was identified as a transcriptional activator of RRAGB.

    Evidence LysoIP proteomics, Co-IP, mTOR activity assays for NUFIP2; RNA pull-down, RIP, ChIP, dual-luciferase, xenograft for circEXOC6B/HIF1A

    PMID:35739524 PMID:36394332

    Open questions at the time
    • Mechanism by which NUFIP2 inhibits Rag nucleotide state not biochemically defined
    • circEXOC6B binding site on RRAGB uncharacterized
    • HIF1A–RRAGB transcriptional axis not validated outside colorectal cancer
  12. 2023 Medium

    RRAGB overexpression was shown to suppress glioblastoma cell proliferation via PI3K/AKT pathway inhibition, revealing a context-dependent tumor-suppressive function distinct from its canonical mTORC1-activating role.

    Evidence RRAGB overexpression in GBM cell lines, PI3K/AKT/mTOR/S6K western blot, AKT activator rescue, xenograft and orthotopic models

    PMID:37517217

    Open questions at the time
    • Mechanism by which RRAGB suppresses PI3K/AKT unclear—may be indirect via mTORC1 negative feedback
    • Not reconciled with RagB's canonical role in mTORC1 activation
    • Single lab, single cancer type

Open questions

Synthesis pass · forward-looking unresolved questions
  • How RRAGB's tumor-suppressive activity via PI3K/AKT inhibition is mechanistically reconciled with its canonical role in mTORC1 activation, and whether RRAGB mutations contribute to human Mendelian disease or are recurrently altered in cancer, remain open questions.
  • No structural model of full-length human RagB–RagC/D heterodimer bound to effectors
  • No direct disease-causing mutations in RRAGB reported
  • Context-dependent pro- versus anti-proliferative roles not mechanistically resolved

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003924 GTPase activity 7
Localization
GO:0005764 lysosome 8
Pathway
R-HSA-162582 Signal Transduction 9 R-HSA-8953897 Cellular responses to stimuli 3 R-HSA-9612973 Autophagy 2
Complex memberships
Rag GTPase heterodimer (RagA/B–RagC/D)Rag–Ragulator complex

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2008 RagB (RRAGB), as part of the heterodimeric Rag GTPase complex, binds raptor (a component of mTORC1) in an amino acid-sensitive manner and is necessary for activation of the mTORC1 pathway by amino acids. A constitutively GTP-bound RagB mutant made mTORC1 resistant to amino acid deprivation, while a GDP-bound mutant prevented amino acid stimulation of mTORC1. The Rag proteins promote intracellular localization of mTOR to a lysosomal compartment containing Rheb without directly stimulating mTORC1 kinase activity. Co-immunoprecipitation, dominant-active/dominant-negative GTPase mutants, subcellular localization imaging Science High 18497260
2010 The Rag GTPases (including RagB/RRAGB) reside on lysosomal membranes via the Ragulator complex (encoded by MAPKSP1, ROBLD3, c11orf59), which recruits the Rags to lysosomes. Amino acids induce mTORC1 movement to lysosomal membranes where active Rag heterodimers reside. Constitutive targeting of mTORC1 to lysosomes rendered mTORC1 amino acid-insensitive and Rag/Ragulator-independent but still Rheb-dependent, placing Rag-Ragulator-mediated lysosomal translocation as the key event in amino acid signaling. Co-immunoprecipitation, lysosomal localization imaging, epistasis with constitutively lysosome-targeted mTORC1 Cell High 20381137
2012 Ragulator functions as a guanine nucleotide exchange factor (GEF) for RagA and RagB (RRAGB), stimulating GTP loading of these GTPases in response to amino acids in a v-ATPase-dependent fashion. Two additional Ragulator components (HBXIP and C7orf59) were identified as required for mTORC1 activation by amino acids. In vitro GEF assay, Co-immunoprecipitation, nucleotide loading assays, genetic knockdown Cell High 22980980
2012 Glutaminolysis (conversion of glutamine to α-ketoglutarate) activates mTORC1 upstream of the Rag GTPases by promoting GTP loading of RagB and lysosomal translocation of mTORC1. Inhibition of glutaminolysis prevented RagB GTP loading; constitutively active Rag heterodimer rescued mTORC1 activation in absence of glutaminolysis, placing RagB downstream of α-ketoglutarate production. Nucleotide loading assays for RagB, epistasis with constitutively active Rag heterodimer, lysosomal translocation imaging Molecular Cell High 22749528
2012 Leucyl-tRNA synthetase (LRS) functions as a GAP (GTPase-activating protein) for Rag GTPases (including RagB/RRAGB) in response to intracellular leucine, binding directly to the Rag GTPase in an amino acid-dependent manner to activate mTORC1 signaling. In vitro GAP assay, Co-immunoprecipitation, mutagenesis of leucine-binding residues of LRS Cell High 22424946
2011 p62/SQSTM1 binds the Rag GTPases (including RagB/RRAGB) in an amino acid-dependent manner, favors formation of the active Rag heterodimer stabilized by raptor, colocalizes with Rags at the lysosomal compartment, and is required for mTORC1 interaction with Rag GTPases and for mTORC1 translocation to the lysosome. Co-immunoprecipitation, co-localization imaging, amino acid-dependent interaction assays, knockdown with mTORC1 activation readouts Molecular Cell High 21981924
2013 GATOR1 (composed of DEPDC5, Nprl2, Nprl3) has GTPase-activating protein (GAP) activity toward RagA and RagB (RRAGB), functioning as a negative regulator of Rag GTPases and hence mTORC1. Inactivating mutations in GATOR1 components in human cancers cause mTORC1 hyperactivation and amino acid insensitivity. In vitro GAP assay, cancer cell line GATOR1 knockdown, amino acid starvation epistasis, mutant analysis Science High 23723238
2000 RagC and RagD were identified as novel GTP-binding proteins that interact with RagA and RagB (RRAGB) via their C-terminal regions (containing a leucine zipper and coiled-coil structure). RagC/D associated with both GDP- and GTP-bound forms of RagA. RagC and RagD changed their subcellular localization depending on the nucleotide-bound state of RagA, establishing the RagA/B–RagC/D heterodimer paradigm. Yeast two-hybrid, GST pulldown, radiolabeled GTP/GDP binding assay, subcellular localization studies Journal of Biological Chemistry High 11073942
2013 Folliculin (FLCN) is recruited to lysosomal surfaces upon amino acid depletion and directly binds RagA/B (including RRAGB) via its GTPase domain, and together with FNIP1 promotes amino acid-dependent mTORC1 recruitment to lysosomes via Rag GTPases. Co-immunoprecipitation, lysosomal localization imaging, amino acid starvation/stimulation assays, FLCN knockout/knockdown Journal of Cell Biology High 24081491
2014 Sestrins bind the heterodimeric RagA/B–RagC/D GTPases and function as guanine nucleotide dissociation inhibitors (GDIs) for RagA/B (including RRAGB), inhibiting amino acid-induced Rag guanine nucleotide exchange and mTORC1 lysosomal translocation. A conserved GDI motif is required; its mutation creates dominant-negative Sestrin rendering mTORC1 insensitive to amino acid deprivation. Co-immunoprecipitation, in vitro GDI assay, mutagenesis of GDI motif, cell-permeable peptide inhibition, mouse knockout Cell High 25259925
2015 SLC38A9, a lysosomal transmembrane amino acid transporter, interacts with Rag GTPases (including RRAGB) and Ragulator in an amino acid-sensitive manner, transporting arginine with high Km. Loss of SLC38A9 represses mTORC1 activation by amino acids (particularly arginine); overexpression of its Ragulator-binding domain renders mTORC1 insensitive to amino acid starvation but not to Rag activity, placing SLC38A9 upstream of the Rag GTPases. Co-immunoprecipitation, amino acid transport assays, lysosomal localization imaging, loss-of-function and gain-of-function genetic epistasis Science High 25561175 25567906
2017 SZT2 recruits a fraction of GATOR1 and GATOR2 to form a SZT2-orchestrated GATOR (SOG) complex essential for GATOR- and Sestrin-dependent nutrient sensing and mTORC1 regulation via Rag GTPases (including RRAGB). SZT2 deficiency causes constitutive mTORC1 signaling under nutrient deprivation; lysosomal localization of SOG is required for its function. Co-immunoprecipitation, lysosomal localization, genetic knockout mouse, epistasis with GATOR1/GATOR2 overexpression Nature High 28199315
2018 TRIM37 interacts with mTOR and RRAGB, enhances the mTOR–RRAGB interaction, and promotes lysosomal localization of mTOR, thereby activating amino acid-stimulated mTORC1 signaling. Loss of TRIM37 reduces TFEB phosphorylation, causing its nuclear translocation and transcriptional activation of lysosome biogenesis and autophagy genes. Co-immunoprecipitation, lysosomal localization imaging, TRIM37 knockdown/knockout, TFEB phosphorylation and nuclear translocation assays Autophagy Medium 29940807
2022 NUFIP2 contributes to mTOR inactivation (via the Ragulator-RRAGA-RRAGB complex) together with LGALS8 (galectin-8) at the lysosome following lysosomal damage. GABARAPs interact directly with NUFIP2 and are required (via Atg8ylation) for NUFIP2 recruitment to damaged lysosomes, where it inhibits the Rag GTPase complex. Proteomic studies of damaged lysosomes, Co-immunoprecipitation, lysosome immunopurification (LysoIP), mTOR activity assays, GABARAP knockout Autophagy Medium 36394332
2022 circEXOC6B (a circular RNA) inhibits the heterodimer formation of RRAGB by directly binding to it, thereby suppressing mTORC1 pathway activity. HIF1A transcriptionally upregulates RRAGB by binding to its promoter, creating a HIF1A-RRAGB-mTORC1 positive feedback loop in colorectal cancer that circEXOC6B can interrupt. RNA pull-down, RNA-binding protein immunoprecipitation, Co-immunoprecipitation, chromatin immunoprecipitation, dual-luciferase assay, in vivo xenograft Molecular Cancer Medium 35739524
2023 RRAGB overexpression in glioblastoma cells reduces proliferation, migration, and invasion and induces G0/G1 cell cycle arrest. RRAGB upregulation decreases expression of PI3K, phosphorylated AKT, mTOR, and S6K; restoring AKT activation rescues GBM cell proliferative and invasive properties, indicating RRAGB suppresses GBM progression partly through blockade of the PI3K/AKT signaling axis. RRAGB overexpression in GBM cell lines, western blot for PI3K/AKT/mTOR/S6K, AKT activator rescue experiment, xenograft and orthotopic mouse models Biochemical and Biophysical Research Communications Medium 37517217
2024 RRAGB is a target of miR-21-3p in endothelial progenitor cells (EPCs); overexpression of RRAGB activates the mTOR pathway, inhibits autophagic activity, and impairs EPC proliferation, migration, and tube formation. Berberine downregulates RRAGB through upregulation of miR-21-3p, restoring EPC function and promoting wound healing. Luciferase reporter assay (miR-21-3p/RRAGB targeting), RRAGB overexpression in EPCs, western blot for mTOR/autophagy markers, EPC functional assays, DVT mouse model Regenerative Therapy Low 39100534
2025 CircMRP4 acts as a sponge for miR-499-5p, leading to upregulation of RRAGB and consequent activation of mTORC1/P70S6K signaling in podocytes under high glucose conditions, promoting podocyte apoptosis and inflammation in diabetic kidney disease. Dual-luciferase reporter, RNA immunoprecipitation, RNA pull-down, RRAGB expression/knockdown, mTORC1/P70S6K western blot, in vivo DKD mouse model Cellular Signalling Low 39842531

Source papers

Stage 0 corpus · 44 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2008 The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science (New York, N.Y.) 2220 18497260
2010 Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 1984 20381137
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2008 Identification of host proteins required for HIV infection through a functional genomic screen. Science (New York, N.Y.) 1165 18187620
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2013 A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1. Science (New York, N.Y.) 884 23723238
2005 The DNA sequence of the human X chromosome. Nature 816 15772651
2012 Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1. Cell 734 22980980
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2015 Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1. Science (New York, N.Y.) 678 25567906
2012 Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway. Cell 665 22424946
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2012 Glutaminolysis activates Rag-mTORC1 signaling. Molecular cell 567 22749528
2015 SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1. Nature 548 25561175
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
2011 p62 is a key regulator of nutrient sensing in the mTORC1 pathway. Molecular cell 426 21981924
2005 Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. Genome research 409 16344560
2016 TRIMs and Galectins Globally Cooperate and TRIM16 and Galectin-3 Co-direct Autophagy in Endomembrane Damage Homeostasis. Developmental cell 386 27693506
2014 Regulation of TORC1 in response to amino acid starvation via lysosomal recruitment of TSC2. Cell 346 24529380
2021 A proximity-dependent biotinylation map of a human cell. Nature 339 34079125
2013 mTOR regulates lysosomal ATP-sensitive two-pore Na(+) channels to adapt to metabolic state. Cell 318 23394946
2013 Recruitment of folliculin to lysosomes supports the amino acid-dependent activation of Rag GTPases. The Journal of cell biology 278 24081491
2012 A high-throughput approach for measuring temporal changes in the interactome. Nature methods 273 22863883
2000 Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B. The Journal of biological chemistry 210 11073942
2015 Dichotomy of Genetic Abnormalities in PEComas With Therapeutic Implications. The American journal of surgical pathology 189 25651471
2014 Sestrins function as guanine nucleotide dissociation inhibitors for Rag GTPases to control mTORC1 signaling. Cell 186 25259925
2007 Integral and associated lysosomal membrane proteins. Traffic (Copenhagen, Denmark) 163 17897319
2017 SZT2 dictates GATOR control of mTORC1 signalling. Nature 159 28199315
2008 Systematic identification of mRNAs recruited to argonaute 2 by specific microRNAs and corresponding changes in transcript abundance. PloS one 148 18461144
2003 Gene expression profile of the human trabecular meshwork: NEIBank sequence tag analysis. Investigative ophthalmology & visual science 141 12766061
2018 TRIM37 deficiency induces autophagy through deregulating the MTORC1-TFEB axis. Autophagy 37 29940807
2022 circEXOC6B interacting with RRAGB, an mTORC1 activator, inhibits the progression of colorectal cancer by antagonizing the HIF1A-RRAGB-mTORC1 positive feedback loop. Molecular cancer 33 35739524
2004 Identification and characterization of human FOXN6, mouse Foxn6, and rat Foxn6 genes in silico. International journal of oncology 30 15202009
2019 A Six-Gene Signature Predicts Survival of Adenocarcinoma Type of Non-Small-Cell Lung Cancer Patients: A Comprehensive Study Based on Integrated Analysis and Weighted Gene Coexpression Network. BioMed research international 28 31886214
2022 Membrane Atg8ylation, stress granule formation, and MTOR regulation during lysosomal damage. Autophagy 22 36394332
2019 Glomerular Proteomic Profiles in the NZB/W F1 Hybrid Mouse Model of Lupus Nephritis. Medical science monitor : international medical journal of experimental and clinical research 6 30900683
2025 Transcriptome Remodeling and Adaptive Preservation of Muscle Protein Content in Hibernating Black Bears. Ecology and evolution 4 40584666
2024 Berberine ameliorates endothelial progenitor cell function and wound healing in vitro and in vivo via the miR-21-3p/RRAGB axis for venous leg ulcers. Regenerative therapy 4 39100534
2025 A Clinicopathologic and Molecular Reappraisal of Myxoinflammatory Fibroblastic Sarcoma-A Controversial and Pathologically Challenging Low-Grade Sarcoma. Genes, chromosomes & cancer 3 39822017
2025 CircMRP4 orchestrates podocytes injury via the miR-499-5p/RRAGB/mTORC1 axis in diabetic kidney disease. Cellular signalling 2 39842531
2025 The Effect of Valine on the Synthesis of α-Casein in MAC-T Cells and the Expression and Phosphorylation of Genes Related to the mTOR Signaling Pathway. International journal of molecular sciences 2 40243924
2025 Transcriptome remodeling and adaptive preservation of muscle protein content in hibernating black bears. bioRxiv : the preprint server for biology 1 40166218
2023 RRAGB-mediated suppression of PI3K/AKT exerts anti-cancer role in glioblastoma. Biochemical and biophysical research communications 0 37517217