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Last update 08 May 2025

IP6K

Last update 08 May 2025

Basic Info

Synonyms

diphosphoinositol pentakisphosphate kinase 1, HISPPD2A, Histidine acid phosphatase domain-containing protein 2A

+ [11]

Introduction

Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when cells are exposed to hyperosmotic stress.

Drugs associated with IP6K

CN119137106

Patent Mining

Target

IP6K x IPMK

Mechanism

IP6K inhibitors [+1]

Active Org.

The University of North Carolina at Chapel Hill

Originator Org.

The University of North Carolina at Chapel Hill

Active Indication

Digestive System Disorders [+3]

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with IP6K

100 Translational Medicine associated with IP6K

0 Patents (Medical) associated with IP6K

265

Literatures (Medical) associated with IP6K

01 May 2025·Journal of Plant Physiology

Overexpression of the tomato nuclear-cytoplasmic shuttling bZIP transcription factor VSF-1 in Arabidopsis retards plant development under mannitol-stressed conditions

Article

Author: Yoon, Hyuk Sung ; Tsugama, Daisuke

VASCULAR SPECIFICITY FACTOR 1 (VSF-1) is a basic leucine zipper transcription factor identified in tomato (Solanum lycopersicum L.). VSF-1 regulates vascular-specific gene expression and is homologous to an Arabidopsis thaliana mechanical stress regulator, VIP1, but physiological roles for VSF-1 remain unclear. Here, we demonstrate that VSF-1 shuttles between the nucleus and the cytoplasm in response to hypo-osmotic stress. In Arabidopsis plants overexpressing the VSF-1-GFP fusion protein, VSF-1-GFP was mainly detected in the cytoplasm under unstressed conditions but in the nucleus under hypo-osmotically stressed conditions. VSF-1 contains three serine residues within HXRXXS motifs, which can serve as its phosphorylation and 14-3-3 protein-binding sites. In a transient gene expression system in Nicotiana benthamiana leaves, GFP-fused VSF-1 variants where those serine residues were replaced with alanine exhibited nuclear accumulation even under unstressed conditions. GFP-fused VSF-1 variants lacking those HXRXXS motifs also exhibited such nuclear accumulation. The VSF-1 variants lacking those HXRXXS motifs failed to interact with 14-3-3 proteins in a yeast two-hybrid system. These findings suggest that the nuclear accumulation of VSF-1 is triggered by hypo-osmotic stress through its dissociation from 14-3-3 proteins, similar to that of VIP1. The Arabidopsis VSF-1-GFP-overexpressing lines exhibited retarded germination and growth in the presence of mannitol, which can induce hyper-osmotic stress and repress nuclear accumulation of VSF-1. These results are consistent with phenotypes from VIP1-GFP-overexpressing lines in a previous study, indicating a conserved role for VIP1 and VSF-1 in regulating osmotic stress responses.

01 Jan 2025·Physiologia Plantarum

Inositol polyphosphates regulate resilient mechanisms in the green alga Chlamydomonas reinhardtii to adapt to extreme nutrient conditions

Article

Author: Personat, José María ; García‐Gómez, María Elena ; Couso, Inmaculada ; Bedera‐García, Rodrigo

AbstractIn the context of climate changing environments, microalgae can be excellent organisms to understand molecular mechanisms that activate survival strategies under stress. Chlamydomonas reinhardtii signalling mutants are extremely useful to decipher which strategies photosynthetic organisms use to cope with changeable environments. The mutant vip1‐1 has an altered profile of pyroinositol polyphosphates (PP‐InsPs), which are signalling molecules present in all eukaryotes and have been connected to P signalling in other organisms including plants, but their implications in other nutrient signalling are still under evaluation. In this study, we conducted prolonged starvation in WT and vip1‐1 Chlamydomonas cells. After N and P had been consumed, they showed important differences in the levels of chlorophyll, photosystem II (PSII) activity and ultrastructural morphology, including differences in the cell size and cell division. Metabolomic analysis under these conditions revealed an overall decrease in different organic compounds such as amino acids, including arginine and its precursors and tryptophan, which is considered a signalling molecule itself in plants. In addition, we observed significant differences in RNA levels of genes related to N assimilation that are under the control of the NIT2 transcription factor. These data are of important relevance in understanding the signalling role of PP‐InsPs in nutrient sensing, especially regarding N, which has not directly been connected to these molecules in green organisms before. Additionally, the PP‐InsPs regulation over cell size and photosynthesis supports novel strategies for the generation of resilient strains, expanding the biotechnological applications of green microalgae.

30 Oct 2024·Bioscience Reports

Interaction with IP6K1 supports pyrophosphorylation of substrate proteins by the inositol pyrophosphate 5-InsP7

Article

Author: Pal, Monisita ; Ladke, Jayashree S. ; Shah, Akruti ; Hamid, Aisha ; Bhandari, Rashna ; Singh, Arpita ; Ganguli, Shubhra

AbstractInositol pyrophosphates (PP-InsPs) are a sub-family of water soluble inositol phosphates that possess one or more diphosphate groups. PP-InsPs can transfer their β-phosphate group to a phosphorylated Ser residue to generate pyrophosphorylated Ser. This unique post-translational modification occurs on Ser residues that lie in acidic stretches within an intrinsically disordered protein sequence. Serine pyrophosphorylation is dependent on the presence of Mg2+ ions, but does not require an enzyme for catalysis. The mechanisms by which cells regulate PP-InsP-mediated pyrophosphorylation are still unknown. We performed mass spectrometry to identify interactors of IP6K1, an enzyme responsible for the synthesis of the PP-InsP 5-InsP7. Interestingly, IP6K1 interacted with several proteins that are known to undergo 5-InsP7-mediated pyrophosphorylation, including the nucleolar proteins NOLC1, TCOF and UBF1, and AP3B1, the β subunit of the AP3 adaptor protein complex. The IP6K1 interactome also included CK2, a protein kinase that phosphorylates Ser residues prior to pyrophosphorylation. We observe the formation of a protein complex between IP6K1, AP3B1, and the catalytic α-subunit of CK2, and show that disrupting IP6K1 binding to AP3B1 lowers its in vivo pyrophosphorylation. We propose that assembly of a substrate-CK2-IP6K complex would allow for coordinated pre-phosphorylation and pyrophosphorylation of the target serine residue, and provide a mechanism to regulate this enzyme-independent modification.

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IP6K

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