Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Isp7 is a novel regulator of amino acid uptake in the TOR signaling pathway


ABSTRACT: We show that the sensitivity of tsc mutant cells to rapamycin is mediated by TORC1 and can be suppressed by overexpression of the 2-oxoglutarate-Fe(II) dependent oxygenase, Isp7. We show that Isp7 is a novel regulator of amino acids uptake that acts via regulation of gene expression, both upstream and downstream of TOR signaling. suppressed by overexpression of the putative 2-oxoglutarate-Fe(II) dependent oxygenase, Isp7. We show that Isp7 is a novel master regulator of amino acids uptake that acts via regulation of gene expression, both upstream and downstream of TOR signaling. TOR proteins reside in two distinct complexes, TOR complex 1 and 2 (TORC1 and TORC2) that are central for the regulation of cellular growth, proliferation and survival. TOR is also the target for the immunosup

ORGANISM(S): Schizosaccharomyces pombe

SUBMITTER: Metsada Pasmanik-Chor 

PROVIDER: E-GEOD-52759 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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