Short on phosphate: plant surveillance and countermeasures

Ticconi, Carla A.; Abel, Steffen

doi:10.1016/j.tplants.2004.09.003

Cited by 247 publications

(207 citation statements)

References 79 publications

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“…Although P is abundant in ecosystems, phosphate (Pi), the form in which P is assimilable, is unevenly distributed in soils, and most soil Pi is immobile and not readily available to roots (Raghothama, 1999). Plants have evolved responses to adapt their growth to conditions of limited Pi supply, one of which is the activation of high-affinity Pi transport, which enhances Pi acquisition (reviewed in Raghothama, 1999;Rausch and Bucher, 2002;Ticconi and Abel, 2004).…”

Section: Introductionmentioning

confidence: 99%

PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 Is a Plant-Specific SEC12-Related Protein That Enables the Endoplasmic Reticulum Exit of a High-Affinity Phosphate Transporter in Arabidopsis [W]

et al. 2005

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PHOSPHATE TRANSPORTER1 (PHT1) genes encode phosphate (Pi) transporters that play a fundamental role in Pi acquisition and remobilization in plants. Mutation of the Arabidopsis thaliana PHOSPHATE TRANSPORTER TRAFFIC FACILITA-TOR1 (PHF1) impairs Pi transport, resulting in the constitutive expression of many Pi starvation-induced genes, increased arsenate resistance, and reduced Pi accumulation. PHF1 expression was detected in all tissues, particularly in roots, flowers, and senescing leaves, and was induced by Pi starvation, thus mimicking the expression patterns of the whole PHT1 gene family. PHF1 was localized in endoplasmic reticulum (ER), and mutation of PHF1 resulted in ER retention and reduced accumulation of the plasma membrane PHT1;1 transporter. By contrast, the PIP2A plasma membrane protein was not mislocalized, and the secretion of Pi starvation-induced RNases was not affected in the mutant. PHF1 encodes a plantspecific protein structurally related to the SEC12 proteins of the early secretory pathway. However, PHF1 lacks most of the conserved residues in SEC12 proteins essential as guanine nucleotide exchange factors. Although it functions in early secretory trafficking, PHF1 likely evolved a novel mechanism accompanying functional specialization on Pi transporters. The identification of PHF1 reveals that plants are also endowed with accessory proteins specific for selected plasma membrane proteins, allowing their exit from the ER, and that these ER exit cofactors may have a phylum-specific origin.

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Section: Introductionmentioning

confidence: 99%

PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 Is a Plant-Specific SEC12-Related Protein That Enables the Endoplasmic Reticulum Exit of a High-Affinity Phosphate Transporter in Arabidopsis [W]

et al. 2005

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“…Pi uptake mechanisms are enhanced at the root/soil interface, particularly through the stimulation of Pi transport activity (Mudge et al, 2002;Shin et al, 2004;Nussaume et al, 2011; Ayadi et al, 2015). In parallel, mobilization of Pi sources from the soil is facilitated by the secretion of acid phosphatases and acidification of the soil surrounding roots (Raghothama, 1999;Plaxton and Tran, 2011;Wang et al, 2011;Zhang et al, 2014; Balzergue et al, 2017).Pi stored within cells also represents an important nutrient source, and plants demonstrate an extraordinary capacity to mobilize these stocks during starvation (Ticconi and Abel, 2004). Vacuoles are the major storage compartment for Pi in the cell (storing about 80% of the total cellular Pi) in nonlimiting conditions (Bieleski, 1983;Poirier and Bucher, 2002).…”

mentioning

confidence: 99%

“…Pi stored within cells also represents an important nutrient source, and plants demonstrate an extraordinary capacity to mobilize these stocks during starvation (Ticconi and Abel, 2004). Vacuoles are the major storage compartment for Pi in the cell (storing about 80% of the total cellular Pi) in nonlimiting conditions (Bieleski, 1983;Poirier and Bucher, 2002).…”

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confidence: 99%

The Phosphate Fast-Responsive Genes PECP1 and PPsPase1 Affect Phosphocholine and Phosphoethanolamine Content

et al. 2018

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Phosphate starvation-mediated induction of the HAD-type phosphatases PPsPase1 (AT1G73010) and PECP1 (AT1G17710) has been reported in Arabidopsis (Arabidopsis thaliana). However, little is known about their in vivo function or impact on plant responses to nutrient deficiency. The preferences of PPsPase1 and PECP1 for different substrates have been studied in vitro but require confirmation in planta. Here, we examined the in vivo function of both enzymes using a reverse genetics approach. We demonstrated that PPsPase1 and PECP1 affect plant phosphocholine and phosphoethanolamine content, but not the pyrophosphate-related phenotypes. These observations suggest that the enzymes play a similar role in planta related to the recycling of polar heads from membrane lipids that is triggered during phosphate starvation. Altering the expression of the genes encoding these enzymes had no effect on lipid composition, possibly due to compensation by other lipid recycling pathways triggered during phosphate starvation. Furthermore, our results indicated that PPsPase1 and PECP1 do not influence phosphate homeostasis, since the inactivation of these genes had no effect on phosphate content or on the induction of molecular markers related to phosphate starvation. A combination of transcriptomics and imaging analyses revealed that PPsPase1 and PECP1 display a highly dynamic expression pattern that closely mirrors the phosphate status. This temporal dynamism, combined with the wide range of induction levels, broad expression, and lack of a direct effect on Pi content and regulation, makes PPsPase1 and PECP1 useful molecular markers of the phosphate starvation response.Plant growth is highly sensitive to a lack of phosphate (Pi); hence, the application of Pi fertilizers has become standard practice for high-throughput crop production (Cordell et al., 2009). Most phosphorus in the soil is not available to plants, as it is combined with other minerals or parts of organic compounds (Bieleski, 1973;Raghothama and Karthikeyan, 2005). Only a small fraction of soluble Pi (usually present at a concentration of ,10 mM in the soil) can be taken up by plants.Although growth is not optimal under limiting conditions, plants can withstand changing Pi concentrations within heterogeneous soils or in the external nutrient supply that can lead to reprogramming of their metabolism and architecture (Hammond et al., 2003;Péret et al., 2011;Plaxton and Tran, 2011). Root architecture can be modified to facilitate Pi uptake by favoring the development of lateral roots (at the expense of primary root elongation in many plants including Arabidopsis), increasing the density and length of root hairs, and limiting the development of aerial parts (López-Bucio et al., 2002;Svistoonoff et al., 2007;Gruber et al., 2013). Pi uptake mechanisms are enhanced at the root/soil interface, particularly through the stimulation of Pi transport activity (Mudge et al., 2002;Shin et al., 2004;Nussaume et al., 2011; Ayadi et al., 2015). In parallel, mobilization of Pi sources fr...

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“…However, most soil Pi is immobile and the Pi concentration available to roots is in micromolar quantities (Raghothama, 1999). To coordinate plant growth with the limited Pi availability, highaffinity Pi transporters have evolved to enable increased Pi acquisition from soils (Raghothama, 1999;Paszkowski et al, 2002;Rausch and Bucher, 2002;Ticconi and Abel, 2004). High-affinity plant Pi transporters were originally identified by sequence similarity with the high-affinity transporter of yeast (Saccharomyces cerevisiae), PHO84.…”

mentioning

confidence: 99%

OsPHF1 Regulates the Plasma Membrane Localization of Low- and High-Affinity Inorganic Phosphate Transporters and Determines Inorganic Phosphate Uptake and Translocation in Rice

et al. 2011

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PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 (PHF1) is known to regulate the plasma membrane localization of PHT1;1, a high-affinity inorganic phosphate (Pi) transporter in Arabidopsis (Arabidopsis thaliana). OsPHF1, a rice (Oryza sativa) gene homologous to AtPHF1, was isolated and found to regulate the localization of both low-and high-affinity Pi transporters to the plasma membrane. Three OsPHF1 allelic mutants carrying one-point mutations at the fifth WD-repeat motif and two at the transmembrane helix, respectively, showed arsenate resistance and severely reduced Pi accumulation. The data indicate that mutation of OsPHF1 results in the endoplasmic reticulum retention of the low-affinity Pi transporter OsPT2 and highaffinity Pi transporter OsPT8. Mutation of OsPHF1 also reduced Pi accumulation in plants exhibiting excessive shoot Pi accumulation due to the overexpression of OsPHR2. However, the transcript level of OsPHF1 itself is not controlled by OsPHR2. Overexpression of OsPHF1 increased Pi accumulation in both roots and shoots in a solution culture with Pi-supplied condition. These results indicate that the role of OsPHF1 is unique in the localization of both low-and high-affinity Pi transporters on the plasma membrane in rice and determines Pi uptake and translocation in rice. The similar function of PHF1 required to facilitate PHT1 transit through the endoplasmic reticulum between Arabidopsis and rice provides an example of expectations from what one would deduce from sequence comparisons to extend knowledge from Arabidopsis to crops.

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Short on phosphate: plant surveillance and countermeasures

Cited by 247 publications

References 79 publications

PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 Is a Plant-Specific SEC12-Related Protein That Enables the Endoplasmic Reticulum Exit of a High-Affinity Phosphate Transporter in Arabidopsis [W]

PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 Is a Plant-Specific SEC12-Related Protein That Enables the Endoplasmic Reticulum Exit of a High-Affinity Phosphate Transporter in Arabidopsis [W]

The Phosphate Fast-Responsive Genes PECP1 and PPsPase1 Affect Phosphocholine and Phosphoethanolamine Content

OsPHF1 Regulates the Plasma Membrane Localization of Low- and High-Affinity Inorganic Phosphate Transporters and Determines Inorganic Phosphate Uptake and Translocation in Rice

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