Inositol pyrophosphate catabolism by three families of phosphatases regulates plant growth and development
Abstract: Inositol pyrophosphates (PP-InsPs) are nutrient messengers whose cellular levels are precisely regulated. Diphosphoinositol pentakisphosphate kinases (PPIP5Ks) generate the active signaling molecule 1,5-InsP8. PPIP5Ks harbor phosphatase domains that hydrolyze PP-InsPs. Plant and Fungi Atypical Dual Specificity Phosphatases (PFA-DSPs) and NUDIX phosphatases (NUDTs) are also involved in PP-InsP degradation. Here, we analyze the relative contributions of the three different phosphatase families to plant PP-InsP catabolism. We report the biochemical characterization of inositol pyrophosphate phosphatases from Arabidopsis and Marchantia polymorpha. Overexpression of different PFA-DSP and NUDT enzymes affects PP-InsP levels and leads to stunted growth phenotypes in Arabidopsis. nudt17/18/21 knock-out mutants have altered PP-InsP pools and gene expression patterns, but no apparent growth defects. In contrast, Marchantia polymorpha Mppfa-dsp1ge, Mpnudt1ge and Mpvip1ge mutants display severe growth and developmental phenotypes and associated changes in cellular PP-InsP levels. Analysis of Mppfa-dsp1geand Mpvip1ge mutants supports a role for PP-InsPs in Marchantia phosphate signaling, and additional functions in nitrate homeostasis and cell wall biogenesis. Simultaneous elimination of two phosphatase activities enhanced the observed growth phenotypes. Taken together, PPIP5K, PFA-DSP and NUDT inositol pyrophosphate phosphatases regulate growth and development by collectively shaping plant PP-InsP pools
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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PLoS Genetics. - 20, 11 (2024) , e1011468, ISSN: 1553-7404
- Event
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Veröffentlichung
- (where)
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Freiburg
- (who)
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Universität
- (when)
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2024
- Creator
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Laurent, Florian
Bartsch, Simon M.
Shukla, Anuj
Rico-Resendiz, Felix
Couto, Daniel
Fuchs, Christelle
Nicolet, Joël
Loubéry, Sylvain
Jessen, Henning Jacob
Fiedler, Dorothea
Hothorn, Michael
- DOI
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10.1371/journal.pgen.1011468
- URN
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urn:nbn:de:bsz:25-freidok-2608212
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:33 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Laurent, Florian
- Bartsch, Simon M.
- Shukla, Anuj
- Rico-Resendiz, Felix
- Couto, Daniel
- Fuchs, Christelle
- Nicolet, Joël
- Loubéry, Sylvain
- Jessen, Henning Jacob
- Fiedler, Dorothea
- Hothorn, Michael
- Universität
Time of origin
- 2024
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Two bifunctional inositol pyrophosphate kinases/phosphatases control plant phosphate homeostasis
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A high-throughput screening-compatible strategy for the identification of inositol pyrophosphate kinase inhibitors : = [Retraction]: A high-throughput screening-compatible strategy for the identification of inositol pyrophosphate kinase inhibitors
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Retraction: A high-throughput screening-compatible strategy for the identification of inositol pyrophosphate kinase inhibitors
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Novel shades of inositol pyrophosphates – in vitro and in cellulo evaluation of inositol pyrophosphate probes
Two bifunctional inositol pyrophosphate kinases/phosphatases control plant phosphate homeostasis
Untersuchungen zur intrazellulären Freisetzung von Nucleosidphosphaten
Inositol pyrophosphate profiling of two HCT116 cell lines uncovers variation in InsP8 levels
Inositol pyrophosphate synthesis by diphosphoinositol pentakisphosphate kinase-1 is regulated by phosphatidylinositol(4,5)bisphosphate
Structures of fission yeast inositol pyrophosphate kinase Asp1 in ligand-free, substrate-bound, and product-bound states
A high-throughput screening-compatible strategy for the identification of inositol pyrophosphate kinase inhibitors : = [Retraction]: A high-throughput screening-compatible strategy for the identification of inositol pyrophosphate kinase inhibitors
Insights into the cellular role of mammalian inositol pyrophosphates
Activities and structure-function analysis of fission yeast inositol pyrophosphate (ipp) kinase-pyrophosphatase asp1 and its impact on regulation of pho1 gene expression
Retraction: A high-throughput screening-compatible strategy for the identification of inositol pyrophosphate kinase inhibitors
The inositol pyrophosphate metabolism of Dictyostelium discoideum does not regulate inorganic polyphosphate (polyP) synthesis
β-lapachone regulates mammalian inositol pyrophosphate levels in an NQO1- and oxygen-dependent manner : = [Beta]-lapachone regulates mammalian inositol pyrophosphate levels in an NQO1- and oxygen-dependent manner
Novel shades of inositol pyrophosphates – in vitro and in cellulo evaluation of inositol pyrophosphate probes
Two bifunctional inositol pyrophosphate kinases/phosphatases control plant phosphate homeostasis
Untersuchungen zur intrazellulären Freisetzung von Nucleosidphosphaten
Inositol pyrophosphate profiling of two HCT116 cell lines uncovers variation in InsP8 levels
Inositol pyrophosphate synthesis by diphosphoinositol pentakisphosphate kinase-1 is regulated by phosphatidylinositol(4,5)bisphosphate
Structures of fission yeast inositol pyrophosphate kinase Asp1 in ligand-free, substrate-bound, and product-bound states
A high-throughput screening-compatible strategy for the identification of inositol pyrophosphate kinase inhibitors : = [Retraction]: A high-throughput screening-compatible strategy for the identification of inositol pyrophosphate kinase inhibitors
Insights into the cellular role of mammalian inositol pyrophosphates
Activities and structure-function analysis of fission yeast inositol pyrophosphate (ipp) kinase-pyrophosphatase asp1 and its impact on regulation of pho1 gene expression
Retraction: A high-throughput screening-compatible strategy for the identification of inositol pyrophosphate kinase inhibitors
The inositol pyrophosphate metabolism of Dictyostelium discoideum does not regulate inorganic polyphosphate (polyP) synthesis