PYP‐1, inorganic pyrophosphatase, is required for larval development and intestinal function in <i>C. elegans</i>

Ko, Kyung Min; Lee, Wonhae; Yu, Jae-Ran; Ahnn, Joohong

doi:10.1016/j.febslet.2007.10.047

Cited by 42 publications

(31 citation statements)

References 34 publications

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“…To obtain the ok753 homozygous animals, we used wts-1(ok753)/dpy-5(e61) daf-16(m26) unc-75(e950) worms. Electron microscopy was performed as previously described (Ko et al, 2007).…”

Section: Electron Microscopymentioning

confidence: 99%

Lats kinase is involved in the intestinal apical membrane integrity in the nematodeCaenorhabditis elegans

Kang

Shin

et al. 2009

Development

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The roles of Lats kinases in the regulation of cell proliferation and apoptosis have been well established. Here we report new roles for Lats kinase in the integrity of the apical membrane structure. WTS-1, the C. elegans Lats homolog, localized primarily to the subapical region in the intestine. A loss-of-function mutation in wts-1 resulted in an early larval arrest and defects in the structure of the intestinal lumen. An electron microscopy study of terminally arrested wts-1 mutant animals revealed numerous microvillicontaining lumen-like structures within the intestinal cells. The wts-1 phenotype was not caused by cell proliferation or apoptosis defects. Instead, we found that the wts-1 mutant animals exhibited gradual mislocalization of apical actin and apical junction proteins, suggesting that wts-1 normally suppresses the formation of extra apical membrane structures. Heat-shock-driven pulsechase expression experiments showed that WTS-1 regulates the localization of newly synthesized apical actins. RNAi of the exocyst complex genes suppressed the mislocalization phenotype of wts-1 mutation. Collectively, the data presented here suggest that Lats kinase plays important roles in the integrity of the apical membrane structure of intestinal cells.

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“…To obtain the ok753 homozygous animals, we used wts-1(ok753)/dpy-5(e61) daf-16(m26) unc-75(e950) worms. Electron microscopy was performed as previously described (Ko et al, 2007).…”

Section: Electron Microscopymentioning

confidence: 99%

Lats kinase is involved in the intestinal apical membrane integrity in the nematodeCaenorhabditis elegans

Kang

Shin

et al. 2009

Development

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“…Similarly, in Saccharomyces cerevisiae, the IPP1 protein is essential for the viability of the yeast cell (Lundin et al, 1991). Moreover, a null mutant of pyp-1, a worm (Caenorhabditis elegans) PPase gene, revealed developmental arrest at early larval stages and exhibited gross defects in intestinal morphology and function (Ko et al, 2007). In Arabidopsis, the V-PPase loss-of-function mutant avp1-1 has been reported to have a severely disrupted development of root, shoot, and flowers and to be infertile (Li et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Keep an Eye on PPi: The Vacuolar-Type H+-Pyrophosphatase Regulates Postgerminative Development inArabidopsis

et al. 2011

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Postgerminative growth of seed plants requires specialized metabolism, such as gluconeogenesis, to support heterotrophic growth of seedlings until the functional photosynthetic apparatus is established. Here, we show that the Arabidopsis thaliana fugu5 mutant, which we show to be defective in AVP1 (vacuolar H + -pyrophosphatase), failed to support heterotrophic growth after germination. We found that exogenous supplementation of Suc or the specific removal of the cytosolic pyrophosphate (PPi) by the heterologous expression of the cytosolic inorganic pyrophosphatase1 (IPP1) gene from budding yeast (Saccharomyces cerevisiae) rescued fugu5 phenotypes. Furthermore, compared with the wild-type and AVP1 Pro :IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant was severely compromised in the dark but recovered upon exogenous supply of Suc to the growth media. Measurements revealed that the peroxisomal b-oxidation activity, dry seed contents of storage lipids, and their mobilization were unaffected in fugu5. By contrast, fugu5 mutants contained ;2.5-fold higher PPi and ;50% less Suc than the wild type. Together, these results provide clear evidence that gluconeogenesis is inhibited due to the elevated levels of cytosolic PPi. This study demonstrates that the hydrolysis of cytosolic PPi, rather than vacuolar acidification, is the major function of AVP1/FUGU5 in planta. Plant cells optimize their metabolic function by eliminating PPi in the cytosol for efficient postembryonic heterotrophic growth.

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“…In microorganisms and invertebrates, it is known that soluble pyrophosphatase activity is necessary for growth and development (Chen et al, 1990;Pérez-Castiñ eira et al, 2002;Islam et al, 2005;Ko et al, 2007). Knowledge about the role of PP i in plant metabolism, however, remains fragmented.…”

Section: Discussionmentioning

confidence: 99%

Virus-Induced Gene Silencing of Plastidial Soluble Inorganic Pyrophosphatase Impairs Essential Leaf Anabolic Pathways and Reduces Drought Stress Tolerance inNicotiana benthamiana

et al. 2010

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The role of pyrophosphate in primary metabolism is poorly understood. Here, we report on the transient down-regulation of plastid-targeted soluble inorganic pyrophosphatase in Nicotiana benthamiana source leaves. Physiological and metabolic perturbations were particularly evident in chloroplastic central metabolism, which is reliant on fast and efficient pyrophosphate dissipation. Plants lacking plastidial soluble inorganic pyrophosphatase (psPPase) were characterized by increased pyrophosphate levels, decreased starch content, and alterations in chlorophyll and carotenoid biosynthesis, while constituents like amino acids (except for histidine, serine, and tryptophan) and soluble sugars and organic acids (except for malate and citrate) remained invariable from the control. Furthermore, translation of Rubisco was significantly affected, as observed for the amounts of the respective subunits as well as total soluble protein content. These changes were concurrent with the fact that plants with reduced psPPase were unable to assimilate carbon to the same extent as the controls. Furthermore, plants with lowered psPPase exposed to mild drought stress showed a moderate wilting phenotype and reduced vitality, which could be correlated to reduced abscisic acid levels limiting stomatal closure. Taken together, the results suggest that plastidial pyrophosphate dissipation through psPPase is indispensable for vital plant processes.Pyrophosphate (PP i ) is a key metabolite generated in the activation of several polymerization steps (Geigenberger et al., 1998;Stitt, 1998;Rojas-Beltrán et al., 1999;Farré et al., 2001;Sonnewald, 2001; Ló pezMarqués et al., 2004), and its removal is essential to prevent the inhibition of thermodynamically unfavorable reactions (Geigenberger et al., 1998; Ló pezMarqués et al., 2004). PP i is generally removed by inorganic pyrophosphatases, which hydrolyze PP i to orthophosphate (P i ). Pyrophosphatases are ubiquitous in plant cells and found both as soluble forms in the cytosol and plastid and as membrane-bound forms on the tonoplast (Rea and Poole, 1993;Baltscheffsky et al., 1999;Maeshima, 2000), mitochondria (Vianello and Macrì, 1999), and chloroplast (Jiang et al., 1997). In Arabidopsis (Arabidopsis thaliana), six soluble pyrophosphatase (sPPase) isoforms have been identified to date (Schulze et al., 2004). Five (AtPPa1, -2, -3, -4, and -5) are far more similar to each other than to AtPPa6 (Schulze et al., 2004) and have been shown to be localized to the cytosol using GFP fusions (Ergen, 2006). In potato (Solanum tuberosum), two sPPase genes, StPPa1 and StPPa2, which are similar to AtPPa1, have also been identified and demonstrated to be present in the cytosol using immunogold labeling (Rojas-Beltrán et al., 1999). In addition to sPPases, several other cytosolic enzymes can remove PP i , including the soluble enzymes pyrophosphate:Fru 6-P phosphotransferase and UDP-Glc pyrophosphorylase. Due to a lack of adverse phenotypic alterations found when altering the expression of these enzymes in auto...

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PYP‐1, inorganic pyrophosphatase, is required for larval development and intestinal function in C. elegans

Cited by 42 publications

References 34 publications

Lats kinase is involved in the intestinal apical membrane integrity in the nematodeCaenorhabditis elegans

Lats kinase is involved in the intestinal apical membrane integrity in the nematodeCaenorhabditis elegans

Keep an Eye on PPi: The Vacuolar-Type H+-Pyrophosphatase Regulates Postgerminative Development inArabidopsis

Virus-Induced Gene Silencing of Plastidial Soluble Inorganic Pyrophosphatase Impairs Essential Leaf Anabolic Pathways and Reduces Drought Stress Tolerance inNicotiana benthamiana

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