Sch9 Is a Major Target of TORC1 in Saccharomyces cerevisiae

Urban, Jörg; Soulard, Alexandre; Huber, Alexandre; Lippman, Soyeon I.; Mukhopadhyay, Debdyuti; Deloche, Olivier; Wanke, Valeria; Anrather, Dorothea; Ammerer, Gustav; Riezman, Howard; Broach, James R.; Virgilio, Claudio De; Hall, Michael N.; Loewith, Robbie

doi:10.1016/j.molcel.2007.04.020

Cited by 740 publications

(1,195 citation statements)

References 42 publications

(54 reference statements)

Supporting

Mentioning

1,112

Contrasting

Unclassified

Order By: Relevance

“…As already described above and illustrated in Fig. 4, the phosphorylation of Sch9 allows TORC1 to prevent the induction of typical G 0 traits as well as to stimulate ribosomal biogenesis and translation initiation (Urban et al 2007;Huber et al 2009). A recent report indicates that TORC1-dependent phosphorylation of Sch9 is subject to feedback control since it is negatively regulated by Sfp1, a transcriptional activator of ribosomal protein and ribi gene expression, which itself is activated by TORC1 (Lempiainen et al 2009).…”

Section: The Protein Kinase Sch9mentioning

confidence: 83%

“…As will be discussed in the section below, several TORC1-mediated processes involve the protein kinase Sch9 (Urban et al 2007). Others appear to be regulated via the PP2A and the PP2A-related protein phosphatases.…”

Section: Rapamycin-sensitive Signalling Via Torc1mentioning

confidence: 99%

“…Here, TORC1 has a dual control. On the one hand, it prevents nuclear translocation of the protein kinase Rim15, thereby ensuring that this kinase is maintained inactive through PKA-mediated phosphorylation (Pedruzzi et al 2003;Urban et al 2007;Wanke et al 2008). Since this control involves Sch9, it will be discussed in more detail in the section below.…”

Section: Rapamycin-sensitive Signalling Via Torc1mentioning

confidence: 99%

“…Yeast contains two PDK1 orthologs, Pkh1 and Pkh2, which, however, contain no PH domain and are apparently activated by sphingolipids rather than by phosphoinositides (Casamayor et al 1999;Friant et al 2001;Liu et al 2005a, b). Sch9 also contains a PDK1 consensus site and it was found that phosphorylation of this site by Pkh1/2 activated Sch9 in vitro (Liu et al 2005a;Urban et al 2007). Moreover, phosphorylation of the PDK1 site appears to be essential for Sch9 to function in vivo for the control of cell growth control and stress resistance (Roelants et al 2004).…”

Section: The Protein Kinase Sch9mentioning

confidence: 99%

“…To date, there are no data that show that Sch9 is a target of the rapamycin-insensitive TORC2. In contrast, Sch9 is directly phosphorylated by TORC1 on at least five residues in the C-terminal half and these phosphorylation events are critical for its catalytic activity (Urban et al 2007). As already described above and illustrated in Fig.…”

Section: The Protein Kinase Sch9mentioning

confidence: 99%

See 4 more Smart Citations

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

et al. 2010

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: The Protein Kinase Sch9mentioning

confidence: 83%

Section: Rapamycin-sensitive Signalling Via Torc1mentioning

confidence: 99%

Section: Rapamycin-sensitive Signalling Via Torc1mentioning

confidence: 99%

Section: The Protein Kinase Sch9mentioning

confidence: 99%

Section: The Protein Kinase Sch9mentioning

confidence: 99%

See 3 more Smart Citations

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

et al. 2010

Self Cite

View full text Add to dashboard Cite

show abstract

Ecm33 is a novel factor involved in efficient glucose uptake for nutrition‐responsive TORC1 signaling in yeast

et al. 2017

View full text Add to dashboard Cite

Glucose uptake is crucial for providing both an energy source and a signal that regulates cell proliferation. Therefore, it is important to clarify the mechanisms underlying glucose uptake and its transmission to intracellular signaling pathways. In this study, we searched for a novel regulatory factor involved in glucose-induced signaling by using Saccharomyces cerevisiae as a eukaryotic model. Requirement of the extracellular protein Ecm33 in efficient glucose uptake and full activation of the nutrient-responsive TOR kinase complex 1 (TORC1) signaling pathway is shown. Cells lacking Ecm33 elicit a series of starvation-induced pathways even in the presence of extracellular high glucose concentration. This results in delayed cell proliferation, reduced ATP, induction of autophagy, and dephosphorylation of the TORC1 substrates Atg13 and Sch9.

show abstract

Plant S6 kinases do not require hydrophobic motif phosphorylation for activity in yeast lacking Ypk3

Yaguchi

Kozaki

2018

FEBS Letters

View full text Add to dashboard Cite

The ribosomal protein S6 kinases (S6K) are among the major substrates and crucial effectors of the target of rapamycin (TOR) kinase, which is an evolutionarily conserved regulator of cell growth and proliferation. Recent research indicates that yeast Ypk3 is an ortholog of mammalian S6Ks. Here, we find that plant S6Ks restore ribosomal protein S6 phosphorylation in a rapamycin-sensitive manner in yeast cells lacking Ypk3. However, phosphorylation of a hydrophobic motif, which is mediated through TOR signaling and essential for mammalian S6K activity, is not detected in plant S6Ks. Furthermore, deletion of the N-terminal region of rice S6Ks shows phosphorylation of the hydrophobic motif and reduced rapamycin sensitivity. Our findings suggest a mechanism of plant S6K activation distinct from that of mammalian S6Ks.

show abstract

Sch9 Is a Major Target of TORC1 in Saccharomyces cerevisiae

Cited by 740 publications

References 42 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

Ecm33 is a novel factor involved in efficient glucose uptake for nutrition‐responsive TORC1 signaling in yeast

Plant S6 kinases do not require hydrophobic motif phosphorylation for activity in yeast lacking Ypk3

Contact Info

Product

Resources

About