Inhibition of the protein kinase A alters the degradation of the high-affinity phosphate transporter Pho84 in Saccharomyces cerevisiae

Mouillon, Jean‐Marie; Persson, Bengt L.

doi:10.1007/s00294-005-0019-0

Cited by 28 publications

(37 citation statements)

References 28 publications

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“…Phosphate transporters are precisely regulated by Pi amount. In plants and yeast, exposure to Pi or nonmetabolized phosphate analogs triggers Pi transporter degradation (Mouillon and Persson, 2005;Bayle et al, 2011). Here we show that in response to As(V), Pi transporters are also delocalized from the plasma membrane to the vacuole, in parallel with the arrest of As(V) uptake.…”

Section: Arabidopsis Plants Have a Sensitive As(v) Perception Mechanismmentioning

confidence: 71%

WRKY6 Transcription Factor Restricts Arsenate Uptake and Transposon Activation in Arabidopsis

et al. 2013

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Stress constantly challenges plant adaptation to the environment. Of all stress types, arsenic was a major threat during the early evolution of plants. The most prevalent chemical form of arsenic is arsenate, whose similarity to phosphate renders it easily incorporated into cells via the phosphate transporters. Here, we found that arsenate stress provokes a notable transposon burst in plants, in coordination with arsenate/phosphate transporter repression, which immediately restricts arsenate uptake. This repression was accompanied by delocalization of the phosphate transporter from the plasma membrane. When arsenate was removed, the system rapidly restored transcriptional expression and membrane localization of the transporter. We identify WRKY6 as an arsenate-responsive transcription factor that mediates arsenate/phosphate transporter gene expression and restricts arsenate-induced transposon activation. Plants therefore have a dual WRKY-dependent signaling mechanism that modulates arsenate uptake and transposon expression, providing a coordinated strategy for arsenate tolerance and transposon gene silencing.

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Section: Arabidopsis Plants Have a Sensitive As(v) Perception Mechanismmentioning

confidence: 71%

WRKY6 Transcription Factor Restricts Arsenate Uptake and Transposon Activation in Arabidopsis

et al. 2013

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“…Although P i availability appears to be the major signal, recent studies have revealed novel components in the regulatory circuit of the PHO responses. It has been shown that, after prolonged P i starvation, the repletion of P i to cells leads to degradation of the high affinity phosphate transporter Pho84 (53,54). This response requires the activation of the protein kinase A (53,54), demonstrating a connection between the glucose and phosphate signaling pathways.…”

Section: Discussionmentioning

confidence: 99%

“…It has been shown that, after prolonged P i starvation, the repletion of P i to cells leads to degradation of the high affinity phosphate transporter Pho84 (53,54). This response requires the activation of the protein kinase A (53,54), demonstrating a connection between the glucose and phosphate signaling pathways. The level of other nutrient intermediates also influences the activation of the PHO pathway.…”

Section: Discussionmentioning

confidence: 99%

Phosphate-responsive Signaling Pathway Is a Novel Component of NAD+ Metabolism in Saccharomyces cerevisiae

Lin

2011

Journal of Biological Chemistry

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Nicotinamide adenine dinucleotide (NADNAD ϩ and its reduced form NADH are essential pyridine nucleotides mediating redox reactions in cellular metabolism. In addition, NAD ϩ is an essential substrate in several protein modification reactions, in particular sirtuin-mediated protein deacetylation and the addition of ADP-ribose moieties. These modifications are essential for the proteins functioning in Ca 2ϩ

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“…Add-back of P i to P i -starved cells normally results in rapid degradation of the Pho84 transporter. However, inhibition of protein kinase A was reported to stabilize Pho84, thereby defining a role for the protein kinase A signal transduction pathway in Pho84 turnover (8). Nonetheless, Pho84 degradation occurs in the vacuole (44) rather than the proteasome, but the pathway by which Pho84 is targeted to the vacuole remains to be elucidated.…”

Section: Discussionmentioning

confidence: 99%

The Rsp5 E3 Ligase Mediates Turnover of Low Affinity Phosphate Transporters in Saccharomyces cerevisiae

Estrella¹,

Krishnamurthy²,

Timme³

et al. 2008

Journal of Biological Chemistry

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In an effort to identify novel components of the PHO regulon in Saccharomyces cerevisiae, we have isolated and characterized suppressors of the Pho ؊ phenotype associated with deletion of the Pho4 transcriptional activator. Here we report that either a defective form of the Rsp5 E3 ubiquitin ligase or deletion of the End3 component of the endocytic pathway restores growth of the pho4⌬ mutant in the presence of limiting inorganic phosphate (P i ). The spa1-1 suppressor allele of RSP5 encodes a phenylalanine-to-valine replacement at position 748 (F748V) within the catalytic HECT domain of Rsp5. Consistent with suppression due to impaired ubiquitin ligase activity, the heat-sensitive growth defect of the spa1-1 mutant is suppressed either by overexpression of ubiquitin or by osmotic stabilization. Western blot analyses revealed that the cellular levels of the Pho87 and Pho91 low affinity P i are markedly increased in the spa1-1 mutant, yet Pho84 high affinity P i transporter levels are unaffected. Furthermore, Pho87 and Pho91 are ubiquitinated in vivo in an Rsp5-dependent manner, and the Pho ؉ phenotype of the spa1-1 suppressor is dependent upon Pho87 and Pho91. We conclude that turnover of the low affinity P i transporters is initiated by Rsp5-mediated ubiquitination followed by internalization and degradation by the endocytic pathway.The yeast Saccharomyces cerevisiae has evolved an elaborate system to sense, acquire, and store inorganic phosphate (P i ) in response to its availability in the extracellular environment (for review, see Refs. 1 and 2). The PHO system consists of (i) the Pho3, Pho5, Pho11, and Pho12 acid phosphatases that are localized to the periplasmic space, (ii) the Pho8 and Pho13 alkaline phosphatases that are localized to the vacuole and periplasm, respectively, (iii) the high affinity plasma membrane P i transporters Pho84 and Pho89, which are regulated in response to P i availability, and the low affinity, constitutively expressed P i transporters Pho87, Pho90, and Pho91, (iv) Git1, a transporter that scavenges glycerophosphoinositol derived from secreted phosphatidylinositol, thereby replenishing inositol, P i , and glycerol (3), and (v) the PHM proteins that are involved in the synthesis and breakdown of polyphosphate, a storage form of P i in the vacuole (for review, see Ref. 4).The PHO regulon is responsible for scavenging P i and has been most extensively studied with regard to regulation of PHO5 expression. The Pho84 transporter and the Pho80 -Pho85 cyclin/cyclin-dependent kinase are negative regulators of PHO5 transcription, whereas the Pho81 inhibitor of Pho80 -Pho85 and the Pho4 transcriptional activator are positive regulators. In the presence of high external concentrations of P i , Pho85 phosphorylates Pho4, resulting in Pho4 nuclear export via the Msn5 exportin and cytoplasmic retention such that PHO5 is repressed (5). Conversely, when P i concentrations are low, Pho81 inhibits Pho85 activity. Pho4 remains unphosphorylated and has high affinity for the Pse1 importin, resulting i...

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Inhibition of the protein kinase A alters the degradation of the high-affinity phosphate transporter Pho84 in Saccharomyces cerevisiae

Cited by 28 publications

References 28 publications

WRKY6 Transcription Factor Restricts Arsenate Uptake and Transposon Activation in Arabidopsis

WRKY6 Transcription Factor Restricts Arsenate Uptake and Transposon Activation in Arabidopsis

Phosphate-responsive Signaling Pathway Is a Novel Component of NAD+ Metabolism in Saccharomyces cerevisiae

The Rsp5 E3 Ligase Mediates Turnover of Low Affinity Phosphate Transporters in Saccharomyces cerevisiae

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