Stp1p, Stp2p and Abf1p are involved in regulation of expression of the amino acid transporter gene BAP3 of Saccharomyces cerevisiae

Boer, Marco de; Nielsen, P. H.; Bebelman, Jan Paul; Heerikhuizen, Harm van; Andersen, H.A.; Planta, Rudi J.

doi:10.1093/nar/28.4.974

Cited by 59 publications

(64 citation statements)

References 30 publications

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“…Upon induction by extracellular amino acids, the SPS sensor catalyzes an endoproteolytic processing event that cleaves the regulatory N-terminal domains. The shorter forms of Stp1 and Stp2 efficiently target to the nucleus where they bind promoters of a limited set of genes, including a subset of broad-specificity amino acid permeases (cluster 1, Table 4) and the peptide transporter Ptr2 (Didion et al 1996(Didion et al , 1998de Boer et al 1998de Boer et al , 2000Iraqui et al 1999;Klasson et al 1999;Wielemans et al 2010;Tumusiime et al 2011).…”

Section: Pathway Genesmentioning

confidence: 99%

Regulation of Amino Acid, Nucleotide, and Phosphate Metabolism in Saccharomyces cerevisiae

2012

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Ever since the beginning of biochemical analysis, yeast has been a pioneering model for studying the regulation of eukaryotic metabolism. During the last three decades, the combination of powerful yeast genetics and genome-wide approaches has led to a more integrated view of metabolic regulation. Multiple layers of regulation, from suprapathway control to individual gene responses, have been discovered. Constitutive and dedicated systems that are critical in sensing of the intra- and extracellular environment have been identified, and there is a growing awareness of their involvement in the highly regulated intracellular compartmentalization of proteins and metabolites. This review focuses on recent developments in the field of amino acid, nucleotide, and phosphate metabolism and provides illustrative examples of how yeast cells combine a variety of mechanisms to achieve coordinated regulation of multiple metabolic pathways. Importantly, common schemes have emerged, which reveal mechanisms conserved among various pathways, such as those involved in metabolite sensing and transcriptional regulation by noncoding RNAs or by metabolic intermediates. Thanks to the remarkable sophistication offered by the yeast experimental system, a picture of the intimate connections between the metabolomic and the transcriptome is becoming clear.

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Section: Pathway Genesmentioning

confidence: 99%

Regulation of Amino Acid, Nucleotide, and Phosphate Metabolism in Saccharomyces cerevisiae

2012

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“…STP2 encodes a transcription factor that controls the expression of genes responsible for the import of amino acids across the plasma membrane (de Boer et al 2000). STP2 has a paralog, STP1, that also plays a redundant role in amino acid transport (de Boer et al 2000); STP1 overexpression (plasmids YGPM10d14 and YGPM17l13) did not suppress sps1*.…”

Section: Screening For High-copy Suppressors Of Sps1mentioning

confidence: 99%

“…STP2 has a paralog, STP1, that also plays a redundant role in amino acid transport (de Boer et al 2000); STP1 overexpression (plasmids YGPM10d14 and YGPM17l13) did not suppress sps1*. As STP2 had no obvious sporulation defect, we chose to focus on SPO77.…”

Section: Screening For High-copy Suppressors Of Sps1mentioning

confidence: 99%

Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae

et al. 2016

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During sporulation in Saccharomyces cerevisiae, a double lipid bilayer called the prospore membrane is formed de novo, growing around each meiotic nucleus and ultimately closing to create four new cells within the mother cell. Here we show that SPS1, which encodes a kinase belonging to the germinal center kinase III family, is involved in prospore membrane development and is required for prospore membrane closure. We find that SPS1 genetically interacts with SPO77 and see that loss of either gene disrupts prospore membrane closure in a similar fashion. Specifically, cells lacking SPS1 and SPO77 produce hyperelongated prospore membranes from which the leading edge protein complex is not removed from the prospore membrane in a timely fashion. The SPS1/ SPO77 pathway is required for the proper phosphorylation and stability of Ssp1, a member of the leading edge protein complex that is removed and degraded when the prospore membrane closes. Genetic dissection of prospore membrane closure finds SPS1 and SPO77 act in parallel to a previously described pathway of prospore membrane closure that involves AMA1, an activator of the meiotic anaphase promoting complex.KEYWORDS prospore membrane; meiotic exit; anaphase promoting complex; sporulation; cytokinesis; germinal center kinase B IOLOGICAL membranes provide a barrier for inhibiting the flow of materials between a cell and its surroundings and for compartmentalizing the contents of the various organelles within a cell. The size and shape of membranes are central to their functions. Membranes are essential for many fundamental cellular processes including ion balance, energy generation, and secretion. In cell division, membrane dynamics are particularly important, where they act to segregate the contents of the cellular progeny.The process of cell division differs among cells. Most commonly, animal cells divide through a mechanism requiring the assembly of an actin-based contractile ring at the division site (reviewed in Green et al. 2012). This actomyosin ring contracts and matures, ultimately leading to scission of the membrane necks mediated by the ESCRTIII (endosomal sorting complex required for transport III) complex. However, other variations of cytokinesis occur: cellularization during early Drosophila embryogenesis, which requires the growth of membranes around the nuclei before the contractile event (Lee and Harris 2014) and cell division in plants, which requires the secretion of vesicles to the division plane to form the phragmoplast, which will eventually separate the two daughter cells (reviewed in Jürgens 2005). Actin is not always involved in cytokinesis; although prokaryotic cells have actin-like filaments (reviewed in Carballido-López 2006), these filaments are not used for cytokinesis (Pollard and Wu 2010). Similarly, cytokinesis in Trypanosoma brucei (a bikont eukaryote) does not require actin but seems to utilize microtubules (Wheeler et al. 2013). In the budding yeast Saccharomyces cerevisiae, an actin-based contractile ring plays a role in ...

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“…Stp1 and Stp2 have been proposed to play redundant roles in the SPS amino acid sensing pathway (18,(21)(22)(23). However, a recent publication suggests that Stp1 and Stp2 are derived from a genome duplication event that occurred in a yeast ancestor and functionally diverged during evolution (25).…”

mentioning

confidence: 99%

Differential Regulation of Transcription Factors Stp1 and Stp2 in the Ssy1-Ptr3-Ssy5 Amino Acid Sensing Pathway

Tumusiime

Zhang

Overstreet

et al. 2011

Journal of Biological Chemistry

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Stp1 and Stp2 are two homologous transcription factors activated in response to extracellular amino acid stimuli. Here we show that both ubiquitin-dependent degradation of Stp1 and Stp2 and their intracellular localization are differentially regulated. We have found that the E2 ubiquitinconjugating enzyme Cdc34 is required for degradation of both full-length and processed Stp1, but not Stp2. We have also found that Grr1, the F-box component of the SCF Grr1 E3 ubiquitin ligase, is the primary factor in degradation of full-length Stp1, whereas both Grr1 and Cdc4 are required for degradation of processed Stp1. Our localization studies showed that full-length Stp1 is localized both in the cytoplasm and at the cell periphery, whereas full-length Stp2 is localized only diffusely in the cytoplasm. We identified two nuclear localization signals of Stp1 and found that the Nterminal domain of Stp1 is required for localization of fulllength Stp1 to the cell periphery. We also found that Stp2 is the primary factor involved in basal activation of target gene expression. Our results indicate that the functions of two seemingly redundant transcription factors can be separated by differential degradation and distinct cellular localization.

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Stp1p, Stp2p and Abf1p are involved in regulation of expression of the amino acid transporter gene BAP3 of Saccharomyces cerevisiae

Cited by 59 publications

References 30 publications

Regulation of Amino Acid, Nucleotide, and Phosphate Metabolism in Saccharomyces cerevisiae

Regulation of Amino Acid, Nucleotide, and Phosphate Metabolism in Saccharomyces cerevisiae

Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae

Differential Regulation of Transcription Factors Stp1 and Stp2 in the Ssy1-Ptr3-Ssy5 Amino Acid Sensing Pathway

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