Regulation of RNA polymerase III transcription involves SCH9-dependent and SCH9-independent branches of the target of rapamycin (TOR) pathway. - Wikidata - wikimedia - TriplyDB

Regulation of RNA polymerase III transcription involves SCH9-dependent and SCH9-independent branches of the target of rapamycin (TOR) pathway.

Regulation of RNA polymerase III transcription involves SCH9-dependent and SCH9-independent branches of the target of rapamycin (TOR) pathway.

http://www.wikidata.org/entity/Q42136973

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Requirement of the mTOR kinase for the regulation of Maf1 phosphorylation and control of RNA polymerase III-dependent transcription in cancer cells mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1 Regulation of pol III transcription by nutrient and stress signaling pathways Codon-biased translation can be regulated by wobble-base tRNA modification systems during cellular stress responses Nutritional control of growth and development in yeast Hydrogen peroxide sensing, signaling and regulation of transcription factors TOR signaling regulates ribosome and tRNA synthesis via LAMMER/Clk and GSK-3 family kinases.Stb3 plays a role in the glucose-induced transition from quiescence to growth in Saccharomyces cerevisiae.Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis.Mtl1 is required to activate general stress response through Tor1 and Ras2 inhibition under conditions of glucose starvation and oxidative stress New suppressors of THO mutations identify Thp3 (Ypr045c)-Csn12 as a protein complex involved in transcription elongation.tRNA biology charges to the front Plasmodium falciparum Maf1 Confers Survival upon Amino Acid Starvation Sch9 regulates ribosome biogenesis via Stb3, Dot6 and Tod6 and the histone deacetylase complex RPD3L.Genome-wide screen for cell growth regulators in fission yeast mTORC1 directly phosphorylates and regulates human MAF1.The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates.Full repression of RNA polymerase III transcription requires interaction between two domains of its negative regulator Maf1 State transitions in the TORC1 signaling pathway and information processing in Saccharomyces cerevisiae Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae.Cell growth- and differentiation-dependent regulation of RNA polymerase III transcription.Casein kinase II-mediated phosphorylation of general repressor Maf1 triggers RNA polymerase III activation.Distinct regulation of Maf1 for lifespan extension by Protein kinase A and Sch9 Sub1 and Maf1, two effectors of RNA polymerase III, are involved in the yeast quiescence cycle.Target of rapamycin (TOR) in nutrient signaling and growth control Differential Phosphorylation of RNA Polymerase III and the Initiation Factor TFIIIB in Saccharomyces cerevisiae.Recovery of RNA polymerase III transcription from the glycerol-repressed state: revisiting the role of protein kinase CK2 in Maf1 phosphoregulation.Genome-Wide Analysis of the TORC1 and Osmotic Stress Signaling Network in Saccharomyces cerevisiae.Covalent small ubiquitin-like modifier (SUMO) modification of Maf1 protein controls RNA polymerase III-dependent transcription repression Environmental signaling through the mechanistic target of rapamycin complex 1: mTORC1 goes nuclear.Maf1 regulation: a model of signal transduction inside the nucleus.MAF1: a new target of mTORC1.Molecular mechanisms linking the evolutionary conserved TORC1-Sch9 nutrient signalling branch to lifespan regulation in Saccharomyces cerevisiae.Exploiting the yeast stress-activated signaling network to inform on stress biology and disease signaling.TORC1-Dependent Phosphorylation Targets in Fission Yeast Nutrient/TOR-dependent regulation of RNA polymerase III controls tissue and organismal growth in Drosophila.Caloric restriction extends yeast chronological lifespan via a mechanism linking cellular aging to cell cycle regulation, maintenance of a quiescent state, entry into a non-quiescent state and survival in the non-quiescent state.Sch9 partially mediates TORC1 signaling to control ribosomal RNA synthesis.PP4 dephosphorylates Maf1 to couple multiple stress conditions to RNA polymerase III repression Does casein kinase II phosphorylation of Maf1 trigger RNA polymerase III activation?

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P2860

Regulation of RNA polymerase III transcription involves SCH9-dependent and SCH9-independent branches of the target of rapamycin (TOR) pathway.

http://www.wikidata.org/entity/Q42136973

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2009 nî lūn-bûn

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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Regulation of RNA polymerase I ...... et of rapamycin (TOR) pathway.

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Regulation of RNA polymerase I ...... hes of the target of rapamycin

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Regulation of RNA polymerase I ...... et of rapamycin (TOR) pathway.

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Regulation of RNA polymerase I ...... hes of the target of rapamycin

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Regulation of RNA polymerase I ...... et of rapamycin (TOR) pathway.

@en

Regulation of RNA polymerase I ...... hes of the target of rapamycin

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Journal of Biological Chemistry

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Regulation of RNA polymerase I ...... et of rapamycin (TOR) pathway.

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Ian M Willis

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Jaehoon Lee

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Robyn D Moir

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P2860

Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.

General repression of RNA polymerase III transcription is triggered by protein phosphatase type 2A-mediated dephosphorylation of Maf1.

The Sch9 kinase is a chromatin-associated transcriptional activator of osmostress-responsive genes.

Sch9 is a major target of TORC1 in Saccharomyces cerevisiae.

Nutrient regulates Tor1 nuclear localization and association with rDNA promoter.

Cell growth control: little eukaryotes make big contributions.

Maf1, a new player in the regulation of human RNA polymerase III transcription.

Maf1 is an essential mediator of diverse signals that repress RNA polymerase III transcription.

Mammalian Maf1 is a negative regulator of transcription by all three nuclear RNA polymerases.

Mapping phosphorylation sites in proteins by mass spectrometry.

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12604-12608

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10.1074/JBC.C900020200

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19

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284

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2009-03-19T00:00:00Z

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19299514

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