Analysis of the SIP3 protein identified in a two-hybrid screen for interaction with the SNF1 protein kinase

Lesage, Pascale; Yang, Xiaolu; Carlson, Marian

doi:10.1093/nar/22.4.597

Cited by 33 publications

(29 citation statements)

References 34 publications

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“…Using a yeast proteome chip, some glycolytic enzymes and glucose transporters were observed to bind phosphoinositides (Zhu et al 2001), consistent with independent reports that most glycolytic enzymes are localized to the cell wall (in addition to the cytoplasm) (Hubbard et al 1994;Lesage et al 1994;Delgado et al 2001;Honigberg and Purnapatre 2003;Willis et al 2003;Young et al 2003). Other work has shown that glucose stimulates cleavage and subsequent signal transduction by the phosphoinositide PI(4,5)P 2 , as well as transcription of INM1 [which encodes a PI(4,5)P 2 biosynthetic enzyme] (Murray and Greenberg 2000).…”

Section: Analysis Of Module Coregulation With Respect To Individual Tsupporting

confidence: 86%

A network of transcriptionally coordinated functional modules in Saccharomyces cerevisiae

Petti¹,

Church²

2005

Genome Res.

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Recent computational and experimental work suggests that functional modules underlie much of cellular physiology and are a useful unit of cellular organization from the perspective of systems biology. Because interactions among modules can give rise to higher-level properties that are essential to cellular function, a complete knowledge of these interactions is necessary for future work in systems biology, including in silico modeling and metabolic engineering. Here we present a computational method for the systematic identification and analysis of functional modules whose activity is coordinated at the level of transcription. We applied this method, Search for Pairwise Interactions (SPIN), to obtain a global view of functional module connectivity in Saccharomyces cerevisiae and to provide insight into the biological mechanisms underlying this coordination. We also examined this global network at higher resolution to obtain detailed information about the interactions of particular module pairs. For instance, our results reveal possible transcriptional coordination of glycolysis and lipid metabolism by the transcription factor Gcr1p, and further suggest that glycolysis and phosphoinositide signaling may regulate each other reciprocally.[Supplemental material is available online at www.genome.org.]The phenotype of a unicellular organism is determined by an integrated network of genes, proteins, and metabolites that participate in reciprocal regulatory relationships. Creating a quantitative description of this network-a goal that has recently engendered the dedicated discipline of systems biology-is essential to understanding, predicting, and manipulating cellular behavior. A first step toward this goal is deciphering the connectivity of the network, that is, the pattern of interactions among its components. Given the complexity of this undertaking, the integrated network is often treated as a group of superimposed subnetworks, including the gene regulatory, protein, and metabolic networks. A corollary task is to determine whether the network's topology reflects its organizational principles. Using biological networks with relatively well-characterized connectivity, quantitative analyses of network topology have revealed that these networks are modular-they can be clustered into nodes that are more densely connected to each other than to nodes in other clusters (Ravasz et al.

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Section: Analysis Of Module Coregulation With Respect To Individual Tsupporting

confidence: 86%

A network of transcriptionally coordinated functional modules in Saccharomyces cerevisiae

Petti¹,

Church²

2005

Genome Res.

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“…The promoters that are activated by Sip4 remain to be identified. Genetic evidence also supports the idea of a functional relationship between Sip3 and the SNF1 pathway (134). DNA-bound LexA-Sip3 fusion proteins activate transcription of a reporter gene, which suggests that Sip3 acts downstream of Snf1.…”

Section: Targets Of Yeast Snf1mentioning

confidence: 52%

“…SIP3 AND SIP4 Other potential targets for the SNF1 complex include Sip3 and Sip4, which were identified in two-hybrid screens using Snf1 as bait (49,134,135). The interaction of Sip4 with the kinase complex is mediated by Gal83 (Vincent and M Carlson, unpublished data).…”

Section: Targets Of Yeast Snf1mentioning

confidence: 99%

THE AMP-ACTIVATED/SNF1 PROTEIN KINASE SUBFAMILY: Metabolic Sensors of the Eukaryotic Cell?

Hardie

Carling

Carlson

1998

Annu. Rev. Biochem.

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1,362

1,347

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Mammalian AMP-activated protein kinase and yeast SNF1 protein kinase are the central components of kinase cascades that are highly conserved between animals, fungi, and plants. The AMP-activated protein kinase cascade acts as a metabolic sensor or "fuel gauge" that monitors cellular AMP and ATP levels because it is activated by increases in the AMP:ATP ratio. Once activated, the enzyme switches off ATP-consuming anabolic pathways and switches on ATP-producing catabolic pathways, such as fatty acid oxidation. The SNF1 complex in yeast is activated in response to the stress of glucose deprivation. In this case the intracellular signal or signals have not been identified; however, SNF1 activation is associated with depletion of ATP and elevation of AMP. The SNF1 complex acts primarily by inducing expression of genes required for catabolic pathways that generate glucose, probably by triggering phosphorylation of transcription factors. SNF1-related protein kinases in higher plants are likely to be involved in the response of plant cells to environmental and/or nutritional stress.

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“…1). To disrupt GIP1 at the chromosomal locus, we first constructed pJT26-HIS by inserting the BamHI fragment from pPL3.1 (46) carrying the HIS3 gene. The BamHI site lies at codon 31 of GIP1.…”

Section: Methodsmentioning

confidence: 99%

Protein Phosphatase Type 1 Interacts with Proteins Required for Meiosis and Other Cellular Processes in Saccharomyces cerevisiae

Song

Carlson

1996

Molecular and Cellular Biology

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Protein phosphatase type 1 (PP1) is involved in diverse cellular processes, and its activity toward specific substrates is thought to be controlled by different regulatory or targeting subunits. To identify regulatory subunits and substrates of the Saccharomyces cerevisiae PP1, encoded by GLC7, we used the two-hybrid system to detect interacting proteins. Among the many proteins identified were Gac1, a known glycogen regulatory subunit, and a protein with homology to Gac1. We also characterized a new gene designated GIP1, for Glc7-interacting protein. We show that a Gip1 fusion protein coimmunoprecipitates with PP1 from cell extracts. Molecular and genetic analyses indicate that GIP1 is expressed specifically during meiosis, affects transcription of late meiotic genes, and is essential for sporulation. Thus, the Gip1 protein is a candidate for a meiosis-specific substrate or regulator of PP1. Finally, we recovered two genes, RED1 and SCD5, with roles in meiosis and the vesicular secretory pathway, respectively. These results provide strong evidence implicating PP1 function in meiosis. In addition, this study indicates that the two-hybrid system offers a promising approach to understanding the multiple roles and interactions of PP1 in cellular regulation.

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Analysis of the SIP3 protein identified in a two-hybrid screen for interaction with the SNF1 protein kinase

Cited by 33 publications

References 34 publications

A network of transcriptionally coordinated functional modules in Saccharomyces cerevisiae

A network of transcriptionally coordinated functional modules in Saccharomyces cerevisiae

THE AMP-ACTIVATED/SNF1 PROTEIN KINASE SUBFAMILY: Metabolic Sensors of the Eukaryotic Cell?

Protein Phosphatase Type 1 Interacts with Proteins Required for Meiosis and Other Cellular Processes in Saccharomyces cerevisiae

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