Arabidopsis PECP1 and PS2 are phosphate starvation-inducible phosphocholine phosphatases

Angkawijaya, Artik Elisa; Nakamura, Yuki

doi:10.1016/j.bbrc.2017.09.094

Cited by 22 publications

(24 citation statements)

References 25 publications

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“…Under phosphate-limiting conditions, cells often substitute DGDG for phospholipids in extra-plastidic membranes (reviewed in: Dormann and Benning 2002; Nakamura 2013). This allows for mobilization of phosphate from phospholipids which act as a phosphate reservoir (Cruz-Ramirez et al 2006;Tjellström et al 2008), and mutants in phospholipid recycling genes show abnormal phenotypes on low-phosphate growth media (Angkawijaya and Nakamura 2017;Gaude et al 2008;Hsueh et al 2017).…”

Section: Contact Sites Between Chloroplasts and Mitochondriamentioning

confidence: 99%

Lipid transport required to make lipids of photosynthetic membranes

2018

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Photosynthetic membranes provide much of the usable energy for life on earth. To produce photosynthetic membrane lipids, multiple transport steps are required, including fatty acid export from the chloroplast stroma to the endoplasmic reticulum, and lipid transport from the endoplasmic reticulum to the chloroplast envelope membranes. Transport of hydrophobic molecules through aqueous space is energetically unfavorable and must be catalyzed by dedicated enzymes, frequently on specialized membrane structures. Here, we review photosynthetic membrane lipid transport to the chloroplast in the context of photosynthetic membrane lipid synthesis. We independently consider the identity of transported lipids, the proteinaceous transport components, and membrane structures which may allow efficient transport. Recent advances in lipid transport of chloroplasts, bacteria, and other systems strongly suggest that lipid transport is achieved by multiple mechanisms which include membrane contact sites with specialized protein machinery. This machinery is likely to include the TGD1, 2, 3 complex with the TGD5 and TGD4/LPTD1 systems, and may also include a number of proteins with domains similar to other membrane contact site lipid-binding proteins. Importantly, the likelihood of membrane contact sites does not preclude lipid transport by other mechanisms including vectorial acylation and vesicle transport. Substantial progress is needed to fully understand all photosynthetic membrane lipid transport processes and how they are integrated.

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Section: Contact Sites Between Chloroplasts and Mitochondriamentioning

confidence: 99%

Lipid transport required to make lipids of photosynthetic membranes

2018

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“…During phosphate starvation, PC is hydrolyzed by phosphate starvation-inducible non-specific phospholipase C4 and 5 (NPC4 and NPC5; Nakamura et al, 2005; Gaude et al, 2008), that provide DAG and PCho. While DAG is the substrate for DGDG biosynthesis, PCho may be dephosphorylated by phosphate starvation-inducible PECP1 and PS2 to produce phosphate and choline (Cho) (Angkawijaya and Nakamura, 2017). Indeed, the double mutant pecp1-1 ps2-3 showed reduced Cho content under phosphate starvation (Angkawijaya and Nakamura, 2017).…”

Section: Resultsmentioning

confidence: 99%

“…While DAG is the substrate for DGDG biosynthesis, PCho may be dephosphorylated by phosphate starvation-inducible PECP1 and PS2 to produce phosphate and choline (Cho) (Angkawijaya and Nakamura, 2017). Indeed, the double mutant pecp1-1 ps2-3 showed reduced Cho content under phosphate starvation (Angkawijaya and Nakamura, 2017). Moreover, overexpression of PECP1 (Hanchi et al, 2018; Tannert et al, 2018) or PS2 (Hanchi et al, 2018) decreased PCho content in planta .…”

Section: Resultsmentioning

confidence: 99%

“…For plate culture, Murashige and Skoog (MS) medium was used at half-strength concentration (Murashige and Skoog, 1962). The pecp1-1 ps2-3 plant was as described previously (Angkawijaya and Nakamura, 2017). For phosphate starvation experiments, medium was prepared according to previous publication (Angkawijaya et al, 2017).…”

Section: Methodsmentioning

confidence: 99%

“…Later, a close homolog of PS2/PPsPase1, named PECP1, was found to be a phosphatase that dephosphorylates major polar head group of phospholipids such as phosphoethanolamine (PEtn) and phosphocholine (PCho) in vitro (May et al, 2012). Although PECP1 but not PS2/PPsPase1 hydrolyzes the phospholipid polar head group in vitro , gene knockout study of the pecp1-1 ps2-3 double mutant (Angkawijaya and Nakamura, 2017) as well as in planta overexpression study (Hanchi et al, 2018) suggest that both are redundant in dephosphorylating the polar head group in vivo . Despite a possible overlapping function of two closely related phosphatases, comparative study on their tissue expression profiles and subcellular localization has not been reported.…”

Section: Introductionmentioning

confidence: 99%

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Expression Profiles of 2 Phosphate Starvation-Inducible Phosphocholine/Phosphoethanolamine Phosphatases, PECP1 and PS2, in Arabidopsis

et al. 2019

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Phosphorus is essential for plant viability. Phosphate-starved plants trigger membrane lipid remodeling to replace membrane phospholipids by non-phosphorus galactolipids presumably to acquire scarce phosphate source. Phosphoethanolamine/phosphocholine phosphatase 1 (PECP1) and phosphate starvation-induced gene 2 (PS2) belong to an emerging class of phosphatase induced by phosphate starvation and dephosphorylates phosphocholine and phosphoethanolamine (PEtn) in vivo . However, detailed spatiotemporal expression pattern as well as subcellular localization has not been investigated yet. Here, by constructing transgenic plants harboring functional translational promoter–reporter fusion system, we showed the expression pattern of PECP1 and PS2 in different tissues and in response to phosphate starvation. Besides, the Venus fluorescent reporter revealed that both are localized at the ER. Characterization of transgenic plants that overexpress PECP1 or PS2 showed that their activity toward PEtn may be different in vivo . We suggest that PECP1 and PS2 are ER-localized phosphatases that show similar expression pattern yet have a distinct substrate specificity in vivo.

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Membrane Homeostasis upon Nutrient (C, N, P) Limitation

Schubotz¹

2018

Biogenesis of Fatty Acids, Lipids and Membranes

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Arabidopsis PECP1 and PS2 are phosphate starvation-inducible phosphocholine phosphatases

Cited by 22 publications

References 25 publications

Lipid transport required to make lipids of photosynthetic membranes

Lipid transport required to make lipids of photosynthetic membranes

Expression Profiles of 2 Phosphate Starvation-Inducible Phosphocholine/Phosphoethanolamine Phosphatases, PECP1 and PS2, in Arabidopsis

Membrane Homeostasis upon Nutrient (C, N, P) Limitation

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