ArticleThe Biochemical journal2011
Receptor-dependent compartmentalization of PPIP5K1, a kinase with a cryptic polyphosphoinositide binding domain.
Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 49 citations in OpenAlex.
- Enhancing inositol pyrophosphate accumulation in plants alters growth, phosphate homeostasis, and insect herbivory.The Plant journal : for cell and molecular biology · 2025Article
- A small signaling domain controls PPIP5K phosphatase activity in phosphate homeostasis.Nature communications · 2025Article
- Article
- Structural and dynamic changes in P-Rex1 upon activation by PIPbioRxiv : the preprint server for biology · 2024Article
- Functions, Mechanisms, and therapeutic applications of the inositol pyrophosphates 5PP-InsPJournal of cardiovascular translational research · 2024Review
- Plant phosphate nutrition: sensing the stress.Stress biology · 2022Review
- Suppressing MDSC Infiltration in Tumor Microenvironment Serves as an Option for Treating Ovarian Cancer Metastasis.International journal of biological sciences · 2022Article
- Inositol Pyrophosphate Pathways and Mechanisms: What Can We Learn from Plants?Molecules (Basel, Switzerland) · 2020Review
- A two-way switch for inositol pyrophosphate signaling: Evolutionary history and biological significance of a unique, bifunctional kinase/phosphatase.Advances in biological regulation · 2020Review
- PPIP5K2 and PCSK1 are Candidate Genetic Contributors to Familial Keratoconus.Scientific reports · 2019Article
- The inositol pyrophosphate pathway in health and diseases.Biological reviews of the Cambridge Philosophical Society · 2018Review
- Inositol Pyrophosphate Synthesis by Diphosphoinositol Pentakisphosphate Kinase-1 is Regulated by Phosphatidylinositol(4,5)bisphosphate.Bioscience reports · 2018Article
- Intimate connections: Inositol pyrophosphates at the interface of metabolic regulation and cell signaling.Journal of cellular physiology · 2018Review
- Mutations in Diphosphoinositol-Pentakisphosphate Kinase PPIP5K2 are associated with hearing loss in human and mouse.PLoS genetics · 2018Article
- Inositol Pyrophosphates: Energetic, Omnipresent and Versatile Signalling Molecules.Journal of the Indian Institute of Science · 2017Review
- The significance of the 1-kinase/1-phosphatase activities of the PPIP5K family.Advances in biological regulation · 2017Review
- Inositol Pyrophosphate Kinase Asp1 Modulates Chromosome Segregation Fidelity and Spindle Function in Schizosaccharomyces pombe.Molecular and cellular biology · 2016Article
- Inositol Polyphosphate Kinases, Fungal Virulence and Drug Discovery.Journal of fungi (Basel, Switzerland) · 2016Review
- Asp1 from Schizosaccharomyces pombe binds a [2Fe-2S](2+) cluster which inhibits inositol pyrophosphate 1-phosphatase activity.Biochemistry · 2015Article
- The emerging roles of inositol pyrophosphates in eukaryotic cell physiology.Journal of biosciences · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The inositol pyrophosphates are multifunctional signalling molecules. One of the families of enzymes that synthesize the inositol pyrophosphates are the Vip1/PPIP5Ks (PP-InsP5 kinases). The kinase domains in Vip1/PPIP5Ks have been mapped to their N-terminus. Each of these proteins also possess a phosphatase-like domain of unknown significance. In the present study, we show that this phosphatase-like domain is not catalytically active. Instead, by using SPR (surface plasmon resonance) to study protein binding to immobilized lipid vesicles, we show that this domain is specialized for binding PtdIns(3,4,5)P3 (PPIP5K1 K(d)=96 nM; PPIP5K2 K(d)=705 nM). Both PtdIns(3,4)P2 and PtdIns(4,5)P2 are significantly weaker ligands, and no significant binding of PtdIns(3,5)P2 was detected. We confirm the functional importance of this domain in inositol lipid binding by site-directed mutagenesis. We present evidence that the PtdIns(3,4,5)P3-binding domain is an unusual hybrid, in which a partial PH (pleckstrin homology) consensus sequence is spliced into the phosphatase-like domain. Agonist-dependent activation of the PtdIns 3-kinase pathway in NIH 3T3 cells drives translocation of PPIP5K1 from the cytosol to the plasma membrane. We have therefore demonstrated receptor-regulated compartmentalization of inositol pyrophosphate synthesis in mammalian cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.