The receptor Msn5 exports the phosphorylated transcription factor Pho4 out of the nucleus

Kaffman, Arie; Rank, Nicole Miller; O’Neill, Elizabeth; Huang, Linda; O’Shea, Erin K.

doi:10.1038/24898

Cited by 317 publications

(273 citation statements)

References 30 publications

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“…Phosphorylated Pho4 then interacts with the export factor Msn5 to be excluded from the nucleus (Kaffman et al 1998a). The first step in activation or repression of the PHO pathway thus occurs via modulation of the activity of the Pho81 CKI.…”

Section: The Protein Kinase Sch9mentioning

confidence: 99%

“…Conversely, TORC1 inactivation triggers (likely due to the activation of protein phosphatases) dephosphorylation of Rim15 at Thr 1075 , thereby favouring accumulation of Rim15 in the nucleus. Since Pho85-Pho80 is mainly localized within the nucleus and TORC1 is predominantly associated with the vacuolar membrane (Kaffman et al 1998a;Sturgill et al 2008), Pho85-Pho80 and TORC1 may act on different pools of Rim15. Interestingly, the intrinsic protein kinase activity of Rim15 is also required for its nuclear export .…”

Section: The Protein Kinase Sch9mentioning

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 Protein Kinase Sch9mentioning

confidence: 99%

Section: The Protein Kinase Sch9mentioning

confidence: 99%

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

et al. 2010

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“…The localization of GR-GFP was monitored in 14 yeast strains each deficient in a different nuclear transport receptor: CRMI (Stade et al, 1997), CSEI (Xiao et al, 1993), Kap95 (Iovine et al, 1995), Kap104 (Aitchison et al, 1996), Kap123 (Seedorf and Silver, 1997), LOS1 (Hopper et al, 1980), MSN5 (Kaffman et al, 1998a), MTR10 (Kadowaki et al, 1994), NMD5 (He and Jacobson, 1995), PSEI (Seedorf and Silver, 1997), SRP1 (Yano et al, 1992), SXM1 (Seedorf and Silver, 1997), Kap114 (Morehouse et al, 1999;Pemberton et al, 1999), and PDR6 (Titov and Blobel, 1999). Yeast strains PSY580, pse1-1, PSY1200, and PSY902 have been described (Seedorf and Silver, 1997).…”

Section: Yeast Strains Handling Transformations and Localization Smentioning

confidence: 99%

Importin 7 and Importin α/Importin β Are Nuclear Import Receptors for the Glucocorticoid Receptor

Freedman

2004

MBoC

192

151

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The vertebrate glucocorticoid receptor (GR) is cytoplasmic without hormone and localizes to the nucleus after hormone binding. GR has two nuclear localization signals (NLS): NL1 is similar in sequence to the SV40 NLS; NL2 is poorly defined, residing in the ligand-binding domain. We found that GR displayed similar hormone-regulated compartmentalization in Saccharomyces cerevisiae and required the Sxm1 nuclear import receptor for NL2-mediated import. Two metazoan homologues of Sxm1, importin 7 and importin 8, bound both NL1 and NL2, whereas importin ␣ selectively bound NL1. In an in vitro nuclear import assay, both importin 7 and the importin ␣-importin ␤ heterodimer could import a GR NL1 fragment. Under these conditions, full-length GR localized to nuclei in the presence but not absence of an unidentified component in cell extracts. Interestingly, importin 7, importin 8, and importin ␣ bound GR even in the absence of hormone; thus, hormonal control of localization is exerted at a step downstream of import receptor binding. INTRODUCTIONTo survive in a complex environment, cells sense external cues and commonly respond by altering gene expression, in part by regulating the intracellular localization and activity of transcriptional regulatory factors. For example, the intracellular localization of the yeast Pho4 and mammalian SREBP factors is altered in response to changes in external phosphate and circulating sterol concentrations, respectively (Kaffman et al., 1998b;Nagoshi et al., 1999). Similarly, changes in blood glucose levels and a wide range of physiological stress signals modulate the circulating level of glucocorticoids, changing the activity and localization of the glucocorticoid receptor (GR). Within minutes of glucocorticoid binding, GR enters the nucleus and activates or represses target gene transcription (Picard and Yamamoto, 1987). However, hormone binding is reversible; after hormone withdrawal, GR locates back to the cytoplasm (t 1/2 ϭ 10 h; Hache et al., 1999).Proteins and RNAs enter and exit the nucleus through the nuclear pore, a 125-MDa complex in the nuclear envelope (Stoffler et al., 1999). Small molecules readily diffuse through the nuclear pore, whereas molecules greater than ϳ40 kDa require import and export machinery for transport (Davis, 1995;Pante and Aebi, 1995). The first nuclear localization sequence (NLS) was identified in the SV40 large T-antigen (Kalderon et al., 1984). Development of an in vitro nuclear import assay facilitated the identification of two proteins that import substrates containing SV40 NLS-like domains. The adapter molecule importin ␣ binds to the NLS of the substrate and the importin ␤ transport receptor, creating a trimeric complex that imports the substrate into the nucleus through the nuclear pore (Strom and Weis, 2001).Based on similarity to importin ␤, a family of nuclear import and export receptors was identified and shown to transport a wide variety of proteins and RNAs into and out of the nucleus. After reaching the nucleoplasm, import receptors bind the...

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“…However, it is clear that auto-and crossregulation of bHLH gene expression, interorganellar movement of bHLH proteins and sequestration of bHLH proteins from binding DNA also play important roles (Ashburner and Lopes, 1995a;Jen et al, 1992;Kaffman et al, 1998aKaffman et al, , 1998bKomeili and O'Shea, 1999;Lin et al, 2000;O'Neill et al, 1996;Robinson and Lopes, 2000b;Ross et al, 2003;Schüller et al, 1992;Schwank et al, 1997;Sekito et al, 2000). S. cerevisiae is an ideal system to evaluate the contribution of each of these mechanisms, since it contains a relatively small number of bHLH proteins.…”

Section: Discussionmentioning

confidence: 99%

“…Lastly, some bHLH proteins are also regulated by cytoplasmic-nuclear shuffling. Rtg3p : Rtg1p and Pho4p are examples of yeast bHLH proteins that translocate to the nucleus under inducing conditions (Kaffman et al, 1998a(Kaffman et al, , 1998bKomeili and O'Shea, 1999;O'Neill et al, 1996;Sekito et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Multiple bHLH proteins regulate CIT2 expression in Saccharomyces cerevisiae

Chen¹,

Lopes²

2010

Yeast

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The basic helix-loop-helix (bHLH) proteins comprise a eukaryotic transcription factor family involved in multiple biological processes. They have the ability to form multiple dimer combinations and most of them also bind a 6 bp site (E-box) with limited specificity. These properties make them ideal for combinatorial regulation of gene expression. The Saccharomyces cerevisiae CIT2 gene, which encodes citrate synthase, was previously known to be induced by the bHLH proteins Rtg1p and Rtg3p in response to mitochondrial damage. Rtg1p-Rtg3p dimers bind two R-boxes (modified E-boxes) in the CIT2 promoter. The current study tested the ability of all nine S. cerevisiae bHLH proteins to regulate the CIT2 gene. The results showed that expression of CIT2-lacZ reporter was induced in a ρ 0 strain by the presence of inositol via the Ino2p and Ino4p bHLH proteins, which are known regulators of phospholipid synthesis. Promoter mutations revealed that inositol induction required a distal E-box in the CIT2 promoter. Interestingly, deleting the INO2, INO4 genes or the cognate E-box revealed phosphate induction of CIT2 expression. This layer of expression required the two R-boxes and the Pho4p bHLH protein, which is known to be required for phosphate-specific regulation. Lastly, the data show that the Hms1p and Sgc1p bHLH proteins also play important roles in repression of CIT2-lacZ expression. Collectively, these results support the model that yeast bHLH proteins coordinate different biological pathways.

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The receptor Msn5 exports the phosphorylated transcription factor Pho4 out of the nucleus

Cited by 317 publications

References 30 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

Importin 7 and Importin α/Importin β Are Nuclear Import Receptors for the Glucocorticoid Receptor

Multiple bHLH proteins regulate CIT2 expression in Saccharomyces cerevisiae

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