Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A mutant of Escherichia coli has been isolated that grows poorly on succinate and exhibits a markedly reduced sensitivity to colicin K. This mutant is also deficient in the respiration-linked transport of proline and thiomethyl-beta-D-galactoside but appears normal for the adenosine triphosphate-dependent transport of glutamine and arginine. A temperature-conditional revertant of the mutant grows on succinate and is sensitive to colicin K at 27 C, but fails to grow on succinate and is insensitive to colicin K at 42 C. Proline transport in the temperature-conditional revertant is reduced at 42 C when either glucose or succinate is used as energy source. Glutamine transport, on the other hand, is normal at 42 C with glucose as energy source, but is reduced with succinate, although not to the same extent as is proline transport. The lack of growth on succinate and the deficiencies in transport at 42 C are not due to a temperature-dependent lesion in either the electron transport chain or in Ca2+, Mg2+-activated adenosine triphosphatase activity. Membrane vesicles prepared from the temperature-conditional revertant are impaired in proline transport at both 27 and 42 C. These findings suggest the existence in the cytoplasmic membrane of E. coli cells of a component, presumably protein, that is required for colicin K action and that functions in respiration-linked and, to a lesser degree, in adenosine triphosphate-dependent active transport systems. This protein may serve as the primary target of colicin K action.
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PMID:Mutant of Escherichia coli defective in response to colicin K and in active transport. 12 54

The mechanistic target of rapamycin (mTOR) complex 1 (mTORC1) integrates environmental and intracellular signals to regulate cell growth. Amino acids stimulate mTORC1 activation at the lysosome in a manner thought to be dependent on the Rag small guanosine triphosphatases (GTPases), the Ragulator complex, and the vacuolar H(+)-adenosine triphosphatase (v-ATPase). We report that leucine and glutamine stimulate mTORC1 by Rag GTPase-dependent and -independent mechanisms, respectively. Glutamine promoted mTORC1 translocation to the lysosome in RagA and RagB knockout cells and required the v-ATPase but not the Ragulator. Furthermore, we identified the adenosine diphosphate ribosylation factor-1 GTPase to be required for mTORC1 activation and lysosomal localization by glutamine. Our results uncover a signaling cascade to mTORC1 activation independent of the Rag GTPases and suggest that mTORC1 is differentially regulated by specific amino acids.
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PMID:Metabolism. Differential regulation of mTORC1 by leucine and glutamine. 2557 8

Mechanistic target of rapamycin complex 1 (mTORC1) is a highly evolutionarily conserved serine/threonine kinase that regulates cell growth and metabolism in response to multiple environmental cues, such as nutrients, hormones, energy, and stress. Deregulation of mTORC1 can lead to diseases such as diabetes, obesity, and cancer. A series of small GTPases, including Rag, Ras homolog enriched in brain (Rheb), adenosine diphosphate ribosylation factor 1 (Arf1), Ras-related protein Ral-A, Ras homolog (Rho), and Rab, are involved in regulating mTORC1 in response to nutrients, and mTORC1 is differentially regulated via these small GTPases according to specific conditions. Leucine and arginine sensing are considered to be well-confirmed amino acid-sensing signals, activating mTORC1 via a Rag GTPase-dependent mechanism as well as the Ragulator complex and vacuolar H+-adenosine triphosphatase (v-ATPase). Glutamine promotes mTORC1 activation via Arf1 independently of the Rag GTPase. In this review, we summarize current knowledge regarding the regulation of mTORC1 activity by small GTPases in response to nutrients, focusing on the function of small GTPases in mTORC1 activation and how small GTPases are regulated by nutrients.
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PMID:Regulation of mTORC1 by Small GTPases in Response to Nutrients. 3196 76