Inositol phosphate synthesis and the nuclear processes they affect

Monserrate, Jessica P.; York, John D.

doi:10.1016/j.ceb.2010.03.006

Cited by 96 publications

(71 citation statements)

References 91 publications

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“…With the exception of InsP 6 (phytic acid), which accumulates to high levels in many plant seeds, higher order InsPs (InsP 4 , InsP 5 , InsP 7 , and InsP 8 ) are typically low abundance molecules with diverse roles in intracellular signaling (Raboy, 2003;Barker et al, 2009;Monserrate and York, 2010;Gillaspy, 2011;Wilson et al, 2013;Williams et al, 2015;Livermore et al, 2016). VIP1 is predicted to pyrophosphorylate InsP 6 at the 1,3 positions, generating 1PP-InsP 5 (In1sP 7 ) and possibly 1,3PP-InsP 4 (InsP8) ( Figure 2C) (Lin et al, 2009).…”

Section: Vip1 Encodes a Predicted Diphosphoinositol Pentakisphosphatementioning

confidence: 99%

Synergism between Inositol Polyphosphates and TOR Kinase Signaling in Nutrient Sensing, Growth Control, and Lipid Metabolism in Chlamydomonas

et al. 2016

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The networks that govern carbon metabolism and control intracellular carbon partitioning in photosynthetic cells are poorly understood. Target of Rapamycin (TOR) kinase is a conserved growth regulator that integrates nutrient signals and modulates cell growth in eukaryotes, though the TOR signaling pathway in plants and algae has yet to be completely elucidated. We screened the unicellular green alga Chlamydomonas reinhardtii using insertional mutagenesis to find mutants that conferred hypersensitivity to the TOR inhibitor rapamycin. We characterized one mutant, vip1-1, that is predicted to encode a conserved inositol hexakisphosphate kinase from the VIP family that pyrophosphorylates phytic acid (InsP 6 ) to produce the low abundance signaling molecules InsP 7 and InsP 8 . Unexpectedly, the rapamycin hypersensitive growth arrest of vip1-1 cells was dependent on the presence of external acetate, which normally has a growth-stimulatory effect on Chlamydomonas. vip1-1 mutants also constitutively overaccumulated triacylglycerols (TAGs) in a manner that was synergistic with other TAG inducing stimuli such as starvation. vip1-1 cells had reduced InsP 7 and InsP 8 , both of which are dynamically modulated in wild-type cells by TOR kinase activity and the presence of acetate. Our data uncover an interaction between the TOR kinase and inositol polyphosphate signaling systems that we propose governs carbon metabolism and intracellular pathways that lead to storage lipid accumulation.

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Section: Vip1 Encodes a Predicted Diphosphoinositol Pentakisphosphatementioning

confidence: 99%

Synergism between Inositol Polyphosphates and TOR Kinase Signaling in Nutrient Sensing, Growth Control, and Lipid Metabolism in Chlamydomonas

et al. 2016

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“…During seed germination, phytate is broken down to myo-inositol, inorganic phosphate, and minerals for seedling growth. InsP 6 can regulate a number of nuclear processes including messenger RNA (mRNA) export, DNA repair, and RNA editing (York, 2006;Monserrate and York, 2010;Lee et al, 2015), and, as a signal molecule, adjust membrane dynamics (di Paolo and de Camilli, 2006;Janetopoulos and Devreotes, 2006;Thole and Nielsen, 2008). However, from a nutritional and environmental point of view, InsP 6 is a major anti-nutrient for livestock and human nutrition because it cannot be digested by monogastric animals, and it also binds to minerals to reduce their bioavailability (Raboy, 2001).…”

Section: Introductionmentioning

confidence: 99%

Tissue-specific expression, developmentally and spatially regulated alternative splicing, and protein subcellular localization of OsLpa1 in rice

Pang

et al. 2016

J. Zhejiang Univ. Sci. B

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Abstract:The OsLpa1 gene (LOC_Os02g57400) was identified to be involved in phytic acid (PA) metabolism because its knockout and missense mutants reduce PA content in rice grain. However, little is known about the molecular characteristics of OsLpa1 in rice and of its homologues in other plants. In the present study, the spatial pattern of OsLpa1 expression was revealed using OsLpa1 promoter::GUS transgenic plants (GUS: β-glucuronidase); GUS histochemical assay showed that OsLpa1 was strongly expressed in stem, leaf, and root tissues, but in floral organ it is expressed mainly and strongly in filaments. In seeds, GUS staining was concentrated in the aleurone layers; a few blue spots were observed in the outer layers of embryo, but no staining was observed in the endosperm. Three OsLpa1 transcripts (OsLpa1.1, OsLpa1.2, OsLpa1.3) are produced due to alternative splicing; quantitative reversetranscriptase polymerase chain reaction (RT-PCR) analysis revealed that the abundance of OsLpa1.3 was negligible compared with OsLpa1.1 and OsLpa1.2 in all tissues. OsLpa1.2 is predominant in germinating seeds (about 5 times that of OsLpa1.1), but its abundance decreases quickly with the development of seedlings and plants, whereas the abundance of OsLpa1.1 rises and falls, reaching its highest level in 45-d-old plants, with abundance greater than that of OsLpa1.2 in both leaves and roots. In seeds, the abundance of OsLpa1 continuously increases with seed growth, being 27.5 and 15 times greater in 28-DAF (day after flowering) seeds than in 7-DAF seeds for OsLpa1.1 and OsLpa1.2, respectively. Transient expression of chimeric genes with green fluorescence protein (GFP) in rice protoplasts demonstrated that all proteins encoded by the three OsLpa1 transcripts are localized to the chloroplast.

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“…Inositol phosphates constitute a family of soluble molecules which play a central role in cell signaling (1)(2)(3). The large variety of inositol phosphate species stems from the attachment of one or more phosphate groups to the six carbon myo-inositol ring.…”

mentioning

confidence: 99%

“…The phosphorylation of inositol 1,4,5-trisphosphate into more complex forms is achieved by inositol kinases of which inositol-polyphosphate multikinase (IPMK) 2 is one of the most relevant. IPMK phosphorylates at positions 3 and 6, converting inositol 1,4,5-trisphosphate to inositol tetrakisphosphate and then inositol tetrakisphosphate to inositol pentakisphosphate (7).…”

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confidence: 99%

Arginine Transcriptional Response Does Not Require Inositol Phosphate Synthesis

Bosch

Saiardi

2012

Journal of Biological Chemistry

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Background:The involvement of inositol phosphates produced by the yeast inositol-polyphosphate multikinase, Arg82, in transcription is controversial. Results: Catalytically inactive Arg82 restores the regulation of arginine-dependent genes in an ARG82 knock-out. Conclusion: Inositol phosphates do not regulate arginine-dependent gene expression. Significance: Independently of its enzymatic activity Arg82 controls arginine-responsive genes.

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Inositol phosphate synthesis and the nuclear processes they affect

Cited by 96 publications

References 91 publications

Synergism between Inositol Polyphosphates and TOR Kinase Signaling in Nutrient Sensing, Growth Control, and Lipid Metabolism in Chlamydomonas

Synergism between Inositol Polyphosphates and TOR Kinase Signaling in Nutrient Sensing, Growth Control, and Lipid Metabolism in Chlamydomonas

Tissue-specific expression, developmentally and spatially regulated alternative splicing, and protein subcellular localization of OsLpa1 in rice

Arginine Transcriptional Response Does Not Require Inositol Phosphate Synthesis

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