TOR Complex 1 Includes a Novel Component, Tco89p (YPL180w), and Cooperates with Ssd1p to Maintain Cellular Integrity in Saccharomyces cerevisiae

Reinke, Aaron W.; Anderson, Scott; McCaffery, J. Michael; Yates, John R.; Aronova, Sofia; Chu, Shaoyan; Fairclough, Stephen R.; Iverson, Cory; Wedaman, Karen P.; Powers, Ted

doi:10.1074/jbc.m313062200

Cited by 230 publications

(315 citation statements)

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“…Several components of the TORC1 and the Tap42-Sit4 complex localize to membranes of the protein secretory pathway (5)(6)(7)(8)(9)(10)(11)(12). Moreover, the EGO-GSE complex, which, in response to amino acids, controls sorting of the general amino acid permease Gap1, and, in combination with TORC1, regulates microautophagy, resides in prevacuolar compartments (29,30).…”

Section: Discussionmentioning

confidence: 99%

“…A prominent role for endogenous membranes of the protein secretory pathway as a platform for Tor signaling has begun to emerge: (i) different components of the Tor protein complexes, termed TORC1 and TORC2, as well as the Tap42-Sit4 phosphatase complex, have been localized to endosomal and vacuolar compartments (5)(6)(7)(8)(9)(10)(11)(12); (ii) a function for the Golgi Ca 2ϩ /Mn 2ϩ ATPase Pmr1 in negatively regulating TORC1 signaling has been demonstrated (13); and (iii) recent studies have shown genetic interactions between TORC1 and different components of the protein-sorting machinery, including those of the class C Vps complex that functions in docking and fusion of vesicles with the Golgi, endosomes, and vacuoles (refs. 9, 14, and reviewed in ref.…”

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confidence: 99%

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Nuclear translocation of Gln3 in response to nutrient signals requires Golgi-to-endosome trafficking in Saccharomyces cerevisiae

Puria

Zurita-Martinez

Cárdenas

2008

Proc. Natl. Acad. Sci. U.S.A.

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The yeast Saccharomyces cerevisiae has developed specialized mechanisms that enable growth on suboptimal nitrogen sources. Exposure of yeast cells to poor nitrogen sources or treatment with the Tor kinase inhibitor rapamycin elicits activation of Gln3 and transcription of nitrogen catabolite-repressed (NCR) genes whose products function in scavenging and metabolizing nitrogen. Here, we show that mutations in class C and D Vps components, which mediate Golgi-to-endosome vesicle transport, impair nuclear translocation of Gln3, NCR gene activation, and growth in poor nitrogen sources. In nutrient-replete conditions, a significant fraction of Gln3 is peripherally associated with light membranes and partially colocalizes with Vps10-containing foci. These results reveal a role for Golgi-to-endosome vesicular trafficking in TORC1-controlled nuclear translocation of Gln3 and support a model in which Tor-mediated signaling in response to nutrient cues occurs in these compartments. These findings have important implications for nutrient sensing and growth control via mTor pathways in metazoans.rapamycin action ͉ Tor signaling

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Nuclear translocation of Gln3 in response to nutrient signals requires Golgi-to-endosome trafficking in Saccharomyces cerevisiae

Puria

Zurita-Martinez

Cárdenas

2008

Proc. Natl. Acad. Sci. U.S.A.

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“…Both Tor1 as well as Tor2 can be found in the multiprotein TORC1 together with Lst8, Kog1 and Tco89. A separate pool of Tor2 also associates with Lst8, Avo1, Avo2, Avo3, Bit61 and Bit2 to form TORC2 (Loewith et al 2002;Chen and Kaiser 2003;Wedaman et al 2003;Reinke et al 2004;Araki et al 2005;Fadri et al 2005). The precise function of these TORinteracting proteins is not known yet.…”

Section: The Tor Pathwaymentioning

confidence: 99%

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

et al. 2010

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Cells of all living organisms contain complex signal transduction networks to ensure that a wide range of physiological properties are properly adapted to the environmental conditions. The fundamental concepts and individual building blocks of these signalling networks are generally well-conserved from yeast to man; yet, the central role that growth factors and hormones play in the regulation of signalling cascades in higher eukaryotes is executed by nutrients in yeast. Several nutrient-controlled pathways, which regulate cell growth and proliferation, metabolism and stress resistance, have been defined in yeast. These pathways are integrated into a signalling network, which ensures that yeast cells enter a quiescent, resting phase (G 0 ) to survive periods of nutrient scarceness and that they rapidly resume growth and cell proliferation when nutrient conditions become favourable again. A series of well-conserved nutrient-sensory protein kinases perform key roles in this signalling network: i.e. Snf1, PKA, Tor1 and Tor2, Sch9 and Pho85-Pho80. In this review, we provide a comprehensive overview on the current understanding of the signalling processes mediated via these kinases with a particular focus on how these individual pathways converge to signalling networks that ultimately ensure the dynamic translation of extracellular nutrient signals into appropriate physiological responses.

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“…First of all, ssd1 is highly pleiotropic. This locus has at least nine different names because of its having been identified in genetic screens for its effect on minichromosome stability, stress tolerance, membrane trafficking, and cell wall integrity, among other things Kosodo et al, 2001;Vannier et al, 2001;Reinke et al, 2004). Systematic global screens have identified ϳ200 genes that show genetic or physical interactions with Ssd1 (Reguly et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Budding YeastSSD1-VRegulates Transcript Levels of Many Longevity Genes and Extends Chronological Life Span in Purified Quiescent Cells

Qin

et al. 2009

MBoC

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Ssd1 is an RNA-binding protein that affects literally hundreds of different processes and is polymorphic in both wild and lab yeast strains. We have used transcript microarrays to compare mRNA levels in an isogenic pair of mutant (ssd1-d) and wild-type (SSD1-V) cells across the cell cycle. We find that 15% of transcripts are differentially expressed, but there is no correlation with those mRNAs bound by Ssd1. About 20% of cell cycle regulated transcripts are affected, and most show sharper amplitudes of oscillation in SSD1-V cells. Many transcripts whose gene products influence longevity are also affected, the largest class of which is involved in translation. Ribosomal protein mRNAs are globally down-regulated by SSD1-V. SSD1-V has been shown to increase replicative life span¤ and we show that SSD1-V also dramatically increases chronological life span (CLS). Using a new assay of CLS in pure populations of quiescent prototrophs, we find that the CLS for SSD1-V cells is twice that of ssd1-d cells. INTRODUCTIONSsd1 is an RNA-binding protein (Uesono et al., 1997;Hogan et al., 2008) that can be distinguished from the hundreds of other RNA-binding proteins by its unusual properties. First of all, ssd1 is highly pleiotropic. This locus has at least nine different names because of its having been identified in genetic screens for its effect on minichromosome stability, stress tolerance, membrane trafficking, and cell wall integrity, among other things Kosodo et al., 2001;Vannier et al., 2001;Reinke et al., 2004). Systematic global screens have identified ϳ200 genes that show genetic or physical interactions with Ssd1 (Reguly et al., 2006). These genes show a striking enrichment (Hong et al., 2008) for posttranslational modifiers (p ϭ 10 Ϫ14 ), including 19 kinases and nine histone deacetylases, and genes involved in the cell cycle and cell morphogenesis (p ϭ 10 Ϫ8 ). ssd1 mutants display sensitivity to high osmolarity, caffeine, fungicides¤ and numerous other compounds, which suggests a role for this protein in the maintenance of cell wall integrity (Ibeas et al., 2001;Parsons et al., 2004), but its mechanism of action remains obscure.Despite, or perhaps because of, its impact on so many different cellular functions, SSD1 is a common site of variation in both laboratory strains and natural populations of budding yeast (Wheeler et al., 2003). One possible explanation is that SSD1-V, which encodes the full-length "wildtype" protein, reduces the virulence of Saccharomyces cerevisiae in one mouse model (Wheeler et al., 2003), but SSD1-V is critical in Candida (Gank et al., 2008) and several fungal pathogens of plants for evading their hosts' defense systems (Tanaka et al., 2007). In most cases, genetic interactions with SSD1-V are positive, whereas the premature termination alleles (ssd1-d) cause lethality or a more extreme phenotype. One important exception is the RAM signaling pathway mutants, tao3 (Du and Novick, 2002), and cbk1 (Tong et al., 2001;Jorgensen et al., 2002), whose loss of function is lethal if the SSD1-V a...

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TOR Complex 1 Includes a Novel Component, Tco89p (YPL180w), and Cooperates with Ssd1p to Maintain Cellular Integrity in Saccharomyces cerevisiae

Cited by 230 publications

References 55 publications

Nuclear translocation of Gln3 in response to nutrient signals requires Golgi-to-endosome trafficking in Saccharomyces cerevisiae

Nuclear translocation of Gln3 in response to nutrient signals requires Golgi-to-endosome trafficking in Saccharomyces cerevisiae

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

Budding YeastSSD1-VRegulates Transcript Levels of Many Longevity Genes and Extends Chronological Life Span in Purified Quiescent Cells

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