Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Phosphorylation regulates myo-inositol-3-phosphate synthase: a novel regulatory mechanism of inositol biosynthesis.

The Journal of biological chemistry - 13 Sept 2013

Deranieh Rania M, He Quan, Caruso Joseph A, Greenberg Miriam L

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Inositol
Share to Intramolecular Lyases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phospholipids

Share to Phosphoproteins

Share to Protein Processing, Post-Translational

Share to Serine

Share to Valproic Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 23902760
DOI: 10.1074/jbc.M113.479121
PMCID: PMC3772229

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phosphorylation regulates myo-inositol-3-phosphate synthase: a novel regulatory mechanism of inositol biosynthesis.PMID 23902760Read ↗

Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast.Semantic proximity Read ↗

Inositol depletion regulates phospholipid metabolism and activates stress signaling in HEK293T cellsSemantic proximity Read ↗

Genome-wide screen for inositol auxotrophy in Saccharomyces cerevisiae implicates lipid metabolism in stress response signaling.Semantic proximity Read ↗

Towards a systematic map of the functional role of protein phosphorylationSemantic proximity Read ↗

Molecular definition of a novel inositol polyphosphate metabolic pathway initiated by inositol 1,4,5-trisphosphate 3-kinase activity in Saccharomyces cerevisiae.Semantic proximity Read ↗

Glycogen synthase kinase-3 is required for optimal de novo synthesis of inositol.Semantic proximity Read ↗

Altering the Phosphorylation Position of Pyrophosphate-Dependent myo-Inositol-1-Kinase Based on Its Crystal Structure.Semantic proximity Read ↗

Expression of yeast INM1 encoding inositol monophosphatase is regulated by inositol, carbon source and growth stage and is decreased by lithium and valproate.Semantic proximity Read ↗

Activities and genetic interactions of fission yeast Aps1, a Nudix-type inositol pyrophosphatase and inorganic polyphosphatase.Semantic proximity Read ↗

The Saccharomyces cerevisiae INO4 gene encodes a small, highly basic protein required for derepression of phospholipid biosynthetic enzymes.Semantic proximity Read ↗

IPMK regulates HDAC3 activity and histone H4 acetylation in human cellsSemantic proximity Read ↗

Inositol pyrophosphates as mammalian cell signals.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.