ArticleThe Journal of biological chemistry2013
Phosphorylation regulates myo-inositol-3-phosphate synthase: a novel regulatory mechanism of inositol biosynthesis.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 50 citations in OpenAlex.
- Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1.Cell stress & chaperones · 2026Article
- Physiological roles of phosphoinositides and inositol phosphates: Implications for metabolic dysfunction-associated steatotic liver disease.Clinical science (London, England : 1979) · 2025Review
- Article
- Disorder-to-order active site capping regulates the rate-limiting step of the inositol pathway.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- DecipheringmSystems · 2024Article
- Valproate regulates inositol synthesis by reducing expression of myo-inositol-3-phosphate synthase.Scientific reports · 2023Article
- Glycine-Induced Phosphorylation Plays a Pivotal Role in Energy Metabolism in Roots and Amino Acid Metabolism in Leaves of Tea Plant.Foods (Basel, Switzerland) · 2023Article
- Inositol depletion regulates phospholipid metabolism and activates stress signaling in HEK293T cells.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2022Article
- Lipidomics Analysis of Outer Membrane Vesicles and Elucidation of the Inositol Phosphoceramide Biosynthetic Pathway in Bacteroides thetaiotaomicron.Microbiology spectrum · 2022Article
- Article
- Role of myo-inositol during skotomorphogenesis in Arabidopsis.Scientific reports · 2020Article
- Wheat Myo-inositol phosphate synthase influences plant growth and stress responses via ethylene mediated signaling.Scientific reports · 2020Article
- Roles of vitamins in stem cells.Cellular and molecular life sciences : CMLS · 2020Review
- Identification of an inositol-3-phosphate synthase 1-B gene (AccIPS1-B) from Apis cerana cerana and its role in abiotic stress.Cell stress & chaperones · 2019Article
- Novel allelic variant of Lpa1 gene associated with a significant reduction in seed phytic acid content in rice (Oryza sativa L.).PloS one · 2019Article
- Valproate inhibits glucose-stimulated insulin secretion in beta cells.Histochemistry and cell biology · 2018Article
- Inositol Depletion Induced by Acute Treatment of the Bipolar Disorder Drug Valproate Increases Levels of Phytosphingosine.The Journal of biological chemistry · 2017Article
- Article
- Valproate Induces the Unfolded Protein Response by Increasing Ceramide Levels.The Journal of biological chemistry · 2016Article
- Myo-inositol phosphate synthase expression in the European eel (Anguilla anguilla) and Nile tilapia (Oreochromis niloticus): effect of seawater acclimation.American journal of physiology. Regulatory, integrative and comparative physiology · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
myo-Inositol-3-phosphate synthase (MIPS) plays a crucial role in inositol homeostasis. Transcription of the coding gene INO1 is highly regulated. However, regulation of the enzyme is not well defined. We previously showed that MIPS is indirectly inhibited by valproate, suggesting that the enzyme is post-translationally regulated. Using (32)Pi labeling and phosphoamino acid analysis, we show that yeast MIPS is a phosphoprotein. Mass spectrometry analysis identified five phosphosites, three of which are conserved in the human MIPS. Analysis of phosphorylation-deficient and phosphomimetic site mutants indicated that the three conserved sites in yeast (Ser-184, Ser-296, and Ser-374) and humans (Ser-177, Ser-279, and Ser-357) affect MIPS activity. Both S296A and S296D yeast mutants and S177A and S177D human mutants exhibited decreased enzymatic activity, suggesting that a serine residue is critical at that location. The phosphomimetic mutations S184D (human S279D) and S374D (human S357D) but not the phosphodeficient mutations decreased activity, suggesting that phosphorylation of these two sites is inhibitory. The double mutation S184A/S374A caused an increase in MIPS activity, conferred a growth advantage, and partially rescued sensitivity to valproate. Our findings identify a novel mechanism of regulation of inositol synthesis by phosphorylation of MIPS.
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