Cloning of a Novel Family of Mammalian GTP-binding Proteins (RagA, RagBs, RagB1) with Remote Similarity to the Ras-related GTPases *
Explore this paper's citation graph
Summary
It is suggested that RagA and RagB are the mammalian homologues of Gtr1 and that they represent a novel subfamily of Ras-homologous GTP binding proteins, presumably involved in phosphate transport and/or cell growth.
- Type
- article
- Published
- 1995-12-01
- Cited by
- 126
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W2081384263
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:36388019
Keywords
Biology, GTP', GTPase, Complementary DNA, Molecular biology
References
No references recorded for this paper.
Cited by
- The ubiquitination of rag A GTPase by RNF152 negatively regulates mTORC1 activation.
- The role of amino acids in liver protein metabolism under a high protein diet : identification of amino acids signal and associated transduction pathways
- Protein S-glutathionylation: new insights on pre-oncogenic cellular model and formulation of a new molecular mechanism
- Interactions moléculaires et cellulaires entre les protéines E3-14.7K, FIP-1 et les microtubules : application dans le transfert de gènes
- A novel 39-kilodalton membrane protein binds GTP in polyomavirus-transformed cells
- Identifizierung eines N-Methyl-N’-nitro-N-Nitrosoguanidin spezifischen mRNA-Expressionsmusters im C3H-M2 Mausfibroblasten-Transformationssystem
- Characterising the signalling mechanism of the mTOR-dependent phosphatase
- Dégradation des fibres pariétales et système xylanolytique de Bacteroides xylanisolvens XB1AT et Roseburia intestinalis XB6B4, espèces bactériennes du microbiote intestinal humain
- Regulation of mTOR complex 1 in response to growth factors and nutrients
- The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation to the deep-sea environment and ecological role in sedimentary organic nitrogen degradation
- Cloning of two splicing variants of the novel Ras-related GTPase Rab29 which is predominantly expressed in kidney.
- Regulation of mTORC1 by amino acids
- Novel G Proteins, Rag C and Rag D, Interact with GTP-binding Proteins, Rag A and Rag B*
- An expanded Ragulator is a GEF for the Rag GTPases that signal amino acid levels to mTORC1
- Crystal Structure of the Gtr1pGTP-Gtr2pGDP Protein Complex Reveals Large Structural Rearrangements Triggered by GTP-to-GDP Conversion*
- The Folliculin tumor suppressor is a GAP for RagC/D GTPases that signal amino acid levels to mTORC1
- Identification of selectively expressed genes and antigens in CTCL
- Rags connect mTOR and autophagy
- Regulation of TORC1 by Rag GTPases in nutrient response
- Current Models of Mammalian Target of Rapamycin Complex 1 (mTORC1) Activation by Growth Factors and Amino Acids
Related papers
- Measurement of the GTPase activity of signal-transducing G-proteins in neuronal membranes.
- Structural insight into the rearrangement of the switch I region in GTP-bound G12A K-Ras.
- Measurement of KRAS-GTPase Activity.
- 1,4‐Dihydropyridines modulate GTP hydrolysis by Go in neuronal membranes
- Exploring potassium-dependent GTP hydrolysis in TEES family GTPases
- Robust colorimetric assays for dynamin's basal and stimulated GTPase activities.
- GTP hydrolysis by human tissue transglutaminase homologue.
- Mutational analysis of Era, an essential GTP-binding protein of Escherichia coli
- Mutational analysis of Era, an essential GTP-binding protein of Escherichia coli.