The SKS1 gene of Saccharomyces cerevisiae is required for long‐term adaptation of snf3 null strains to low glucose

Vagnoli, Paola; Bisson, Linda F.

doi:10.1002/(sici)1097-0061(19980315)14:4<359::aid-yea227>3.3.co;2-r

Cited by 6 publications

(6 citation statements)

References 18 publications

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“…Fus3 is not known to enter the nucleus in response to nutrient limitation, and this result was unexpected. Sks1 is involved in the cellular response to glucose limitation (Vagnoli and Bisson 1998) and Ksp1 is poorly characterized. The surprising finding came when it was discovered that the colocalization of these kinases was interdependent (Bharucha et al 2008).…”

Section: Mechanisms Of Signal Integration During Filamentous Growthmentioning

confidence: 99%

The Regulation of Filamentous Growth in Yeast

2012

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Filamentous growth is a nutrient-regulated growth response that occurs in many fungal species. In pathogens, filamentous growth is critical for host-cell attachment, invasion into tissues, and virulence. The budding yeast Saccharomyces cerevisiae undergoes filamentous growth, which provides a genetically tractable system to study the molecular basis of the response. Filamentous growth is regulated by evolutionarily conserved signaling pathways. One of these pathways is a mitogen activated protein kinase (MAPK) pathway. A remarkable feature of the filamentous growth MAPK pathway is that it is composed of factors that also function in other pathways. An intriguing challenge therefore has been to understand how pathways that share components establish and maintain their identity. Other canonical signaling pathways-rat sarcoma/protein kinase A (RAS/PKA), sucrose nonfermentable (SNF), and target of rapamycin (TOR)-also regulate filamentous growth, which raises the question of how signals from multiple pathways become integrated into a coordinated response. Together, these pathways regulate cell differentiation to the filamentous type, which is characterized by changes in cell adhesion, cell polarity, and cell shape. How these changes are accomplished is also discussed. High-throughput genomics approaches have recently uncovered new connections to filamentous growth regulation. These connections suggest that filamentous growth is a more complex and globally regulated behavior than is currently appreciated, which may help to pave the way for future investigations into this eukaryotic cell differentiation behavior. TABLE OF CONTENTS Abstract 23Introduction 24

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Section: Mechanisms Of Signal Integration During Filamentous Growthmentioning

confidence: 99%

The Regulation of Filamentous Growth in Yeast

2012

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“…Fus3p is the MAPK mediating the yeast mating response (Elion et al, 1993;Choi et al, 1999), and Sks1p is a serine/threonine kinase involved in the cellular response to glucose limitation (Vagnoli and Bisson, 1998). The cellular function of Ksp1p is unknown, although its overexpression is known to suppress mutations in SRM1, a nucleotide exchange factor required for nucleocytoplasmic trafficking of macromolecules (Fleischmann et al, 1996).…”

Section: Localization Of Yeast Kinases During Filamentous Growthmentioning

confidence: 99%

Analysis of the Yeast Kinome Reveals a Network of Regulated Protein Localization during Filamentous Growth

Bharucha

Dobry

et al. 2008

MBoC

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The subcellular distribution of kinases and other signaling proteins is regulated in response to cellular cues; however, the extent of this regulation has not been investigated for any gene set in any organism. Here, we present a systematic analysis of protein kinases in the budding yeast, screening for differential localization during filamentous growth. Filamentous growth is an important stress response involving mitogen-activated protein kinase and cAMP-dependent protein kinase signaling modules, wherein yeast cells form interconnected and elongated chains. Because standard strains of yeast are nonfilamentous, we constructed a unique set of 125 kinase-yellow fluorescent protein chimeras in the filamentous ⌺1278b strain for this study. In total, we identified six cytoplasmic kinases (Bcy1p, Fus3p, Ksp1p, Kss1p, Sks1p, and Tpk2p) that localize predominantly to the nucleus during filamentous growth. These kinases form part of an interdependent, localization-based regulatory network: deletion of each individual kinase, or loss of kinase activity, disrupts the nuclear translocation of at least two other kinases. In particular, this study highlights a previously unknown function for the kinase Ksp1p, indicating the essentiality of its nuclear translocation during yeast filamentous growth. Thus, the localization of Ksp1p and the other kinases identified here is tightly controlled during filamentous growth, representing an overlooked regulatory component of this stress response. INTRODUCTIONIn eukaryotes, protein function is regulated through mechanisms controlling transcription, translation, post-translational modification, protein degradation, and subcellular localization. In recent years, global studies, systematic studies, or both have been used to consider the majority of these regulatory mechanisms across a wide set of genes and proteins. DNA microarray technologies (DeRisi et al., 1997;Gasch et al., 2001) and mass spectrometry-based approaches (Gygi et al., 1999;Tang et al., 2005;Roth et al., 2006) have cataloged genome-wide changes in transcriptional levels, protein abundance, and posttranslational modifications; however, our understanding of regulated protein localization remains cursory, constructed piecemeal from individual reports of a given protein whose function is regulated by its localization.Protein localization has been investigated most intensely in Saccharomyces. cerevisiae (Kumar et al., 2002;Huh et al., 2003), and reports of regulated protein localization have surfaced frequently in yeast-based studies. For example, several yeast proteins, such as the G1 cyclins Cln2p and Cln3p, are regulated by differential compartmentalization during cell cycle progression (Edgington and Futcher, 2001). The transcription factor Pho4p, involved in phosphate metabolism, is predominantly cytoplasmic under conditions of phosphate sufficiency, but it localizes to the nucleus during phosphate starvation (O'Neill et al., 1996). Components of the yeast Slt2p mitogen-activated protein kinase (MAPK) cell wall integrity ...

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“…the direct target of Grr1 in this process, we have evaluated the regulation of Rgt1 phosphorylation in cells carrying deficiencies in protein kinases with known roles in the specific regulation of HXT gene expression or with general roles in the regulation of carbohydrate metabolism. These included, but were not limited to SKS1 (Yang and Bisson, 1996;Vagnoli and Bisson, 1998), its close homolog VHS1 (YDR247W), SNF1 (Hardie et al, 1998), and TPK1, TPK2 and TPK3 (Toda and Sass, 1988). None of the kinases analyzed exhibited a substantial defect in the glucose-induced phosphorylation of Rgt1 (our unpublished data).…”

Section: Grr1 Regulation Of Rgt1 Phosphorylation and Promoter Bindingmentioning

confidence: 99%

Grr1-dependent Inactivation of Mth1 Mediates Glucose-induced Dissociation of Rgt1 from HXT Gene Promoters

Flick

Spielewoy

Kalashnikova

et al. 2003

MBoC

144

196

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In budding yeast, HXT genes encoding hexose permeases are induced by glucose via a mechanism in which the F box protein Grr1 antagonizes activity of the transcriptional repressor Rgt1. Neither the mechanism of Rgt1 inactivation nor the role of Grr1 in that process has been understood. We show that glucose promotes phosphorylation of Rgt1 and its dissociation from HXT gene promoters. This cascade of events is dependent upon the F-box protein Grr1. Inactivation of Rgt1 is sufficient to explain the requirement for Grr1 but does not involve Rgt1 proteolysis or ubiquitination. We show that inactivation of Mth1 and Std1, known negative regulators of HXT gene expression, leads to the hyperphosphorylation of Rgt1 and its dissociation from HXT promoters even in the absence of glucose. Furthermore, inactivation of Mth1 and Std1 bypasses the requirement for Grr1 for induction of these events, suggesting they are targets for inactivation by Grr1. Consistent with that proposal, Mth1 is rapidly eliminated in response to glucose via a mechanism that requires Grr1. Based upon these data, we propose that glucose acts via Grr1 to promote the degradation of Mth1. Degradation of Mth1 leads to phosphorylation and dissociation of Rgt1 from HXT promoters, thereby activating HXT gene expression.

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The SKS1 gene of Saccharomyces cerevisiae is required for long‐term adaptation of snf3 null strains to low glucose

Cited by 6 publications

References 18 publications

The Regulation of Filamentous Growth in Yeast

The Regulation of Filamentous Growth in Yeast

Analysis of the Yeast Kinome Reveals a Network of Regulated Protein Localization during Filamentous Growth

Grr1-dependent Inactivation of Mth1 Mediates Glucose-induced Dissociation of Rgt1 from HXT Gene Promoters

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