Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression

Kunz, Jeannette; Henríquez, Rubén; Schneider, Ulrich; Deuter-Reinhard, Maja; Movva, N. Rao; Hall, Michael N.

doi:10.1016/0092-8674(93)90144-f

Cited by 785 publications

(578 citation statements)

References 71 publications

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“…Structural aspects and localization of the TOR protein complexes TOR1 and TOR2 encode two large (*280 kDa) and homologous (67% identical) proteins that belong to a family of phosphatidylinositol kinase-related kinases (PIKKs) (Cafferkey et al 1993;Kunz et al 1993;Helliwell et al 1994;Keith and Schreiber 1995). Despite their resemblance to lipid kinases, they are thought to function solely as Ser/Thr protein kinases.…”

Section: The Tor Pathwaymentioning

confidence: 99%

“…Interestingly, the constitution of TORC1 appears to be unaffected by rapamycin, implying that rapamycin does not inhibit TORC1 signalling by interfering with TORC1 stability (Loewith et al 2002). Both TOR complexes are essential for viability, since deletion of TOR2 (inactivation of TORC2) or deletion of both TOR1 and TOR2, or rapamycin treatment (inactivation of TORC1) are lethal to yeast (Heitman et al 1991;Kunz et al 1993). Deletion of TOR1 alone, however, is not lethal, indicating that Tor1 and Tor2 have a redundant role in TORC1 signalling.…”

Section: The Tor Pathwaymentioning

confidence: 99%

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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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Section: The Tor Pathwaymentioning

confidence: 99%

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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“…Functionally, PI-3 kinase-related proteins can be divided into two groups. The ®rst group includes the S. cerevisiae TOR1 and TOR2 proteins and mammalian homologs FRAP/RAFT1/mTOR, all of which participate in G1/S cell cycle progression and are targets for the rapamycin-FKBP12 complex (Kunz et al, 1993;Helliwell et al, 1994;Brown et al, 1994;Sabatini et al, 1994;Sabers et al, 1995). In general, the other family members are necessary for proper responses to DNA damage and cells individually lacking expression of several of these gene products share many of the same phenotypes as AT cells.…”

Section: Atm Proteinmentioning

confidence: 99%

The role of ATM in DNA damage responses and cancer

1998

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“…Strains and plasmids S. cerevisiae strains were derivatives of the haploid strain JK9-3da (leu2-3,112 ura3-52 rme1 trp1 his4) [55]. These cells were grown in rich glucose medium (YPD) supplemented with 20 μg/mL each of adenine and uracil, or in minimal glucose dropout medium (SD) [56] prepared using nutrient mixtures from Sunrise Science Products.…”

Section: Methodsmentioning

confidence: 99%

Secretion of a foreign protein from budding yeasts is enhanced by cotranslational translocation and by suppression of vacuolar targeting

Fitzgerald

Glick

2014

Microb Cell Fact

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Background: Budding yeasts are often used to secrete foreign proteins, but the efficiency is variable. To identify roadblocks in the yeast secretory pathway, we used a monomeric superfolder GFP (msGFP) as a visual tracer in Saccharomyces cerevisiae and Pichia pastoris. Results: One roadblock for msGFP secretion is translocation into the ER. Foreign proteins are typically fused to the bipartite α-factor secretion signal, which consists of the signal sequence followed by the pro region. The α-factor signal sequence directs posttranslational translocation. For msGFP, posttranslational translocation is inefficient with the α-factor signal sequence alone but is stimulated by the pro region. This requirement for the pro region can be bypassed by using the Ost1 signal sequence, which has been shown to direct cotranslational translocation. A hybrid secretion signal consisting of the Ost1 signal sequence followed by the α-factor pro region drives efficient translocation followed by rapid ER export. A second roadblock for msGFP secretion in S. cerevisiae occurs during exit from the Golgi, when some of the msGFP molecules are diverted to the vacuole. Deletion of the sorting receptor Vps10 prevents vacuolar targeting of msGFP at the expense of missorting vacuolar hydrolases such as carboxypeptidase Y (CPY) to the culture medium. However, a truncation of Vps10 blocks vacuolar targeting of msGFP while permitting CPY to be sorted normally. Conclusions: With budding yeasts, if the secretion or processing of a foreign protein is poor, we recommend two options. First, use the Ost1 signal sequence to achieve efficient entry into the secretory pathway while avoiding the processing issues associated with the α-factor pro region. Second, truncate Vps10 to suppress diversion to the vacuole. These insights obtained with msGFP highlight the value of applying cell biological methods to study yeast secretion.

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Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression

Cited by 785 publications

References 71 publications

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

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

The role of ATM in DNA damage responses and cancer

Secretion of a foreign protein from budding yeasts is enhanced by cotranslational translocation and by suppression of vacuolar targeting

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