GO:0005545 1-phosphatidylinositol binding: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0005545 defines the molecular function of binding to phosphatidylinositol, a glycophospholipid with its sn-glycerol 3-phosphate residue esterified to the 1-hydroxyl group of 1D-myo-inositol.
• This binding activity is central to the recruitment and regulation of phosphatidylinositol 4-kinases (PI4Ks) and phosphatidylinositol phosphate kinases (PIPKs) at specific membrane compartments [1,4].
• PI4KB, a key enzyme that binds phosphatidylinositol, is recruited to Golgi membranes by ARMH3 to direct Golgi-to-endosome trafficking and STING activation.
• Golgi-localized PI4KB also mediates Rab11a activation and trafficking to promote ciliogenesis.
• Palmitoylation targets calcineurin to the phosphatidylinositol 4-kinase complex at the plasma membrane, illustrating how 1-phosphatidylinositol binding is regulated by lipid modifications.
• Dysregulation of phosphatidylinositol-binding proteins is linked to immune signaling defects, ciliopathies, and cancer, making these proteins attractive therapeutic targets [1,2].
Description
Phosphatidylinositol (PI) is a minor but critically important glycerophospholipid in eukaryotic membranes. The molecular function defined by GO:0005545, 1-phosphatidylinositol binding, refers to the selective interaction of a protein with the inositol headgroup of PI, where the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. This binding event is the first step in a cascade of lipid signaling and membrane trafficking events that control cell growth, immune responses, and organelle identity [1,4]. Researchers study this function because it determines where and when lipid kinases and their effectors assemble, thereby influencing diseases ranging from cancer to ciliopathies [1,2]. The binding is not merely a passive tether; it often induces conformational changes that activate enzymes such as phosphatidylinositol 4-kinases (PI4Ks) and phosphatidylinositol phosphate kinases (PIPKs) [4,5]. Understanding the structural and regulatory features of 1-phosphatidylinositol binding is therefore essential for decoding membrane signaling networks and for developing targeted therapeutics.
1-phosphatidylinositol binding At A Glance
| GO ID | GO:0005545 |
|---|---|
| GO term | 1-phosphatidylinositol binding |
| Ontology | molecular_function |
| Synonym | None |
| Major function | Binding to phosphatidylinositol, a glycophospholipid with its sn-glycerol 3-phosphate residue esterified to the 1-hydroxyl group of 1D-myo-inositol |
| Related enzymes | Phosphatidylinositol 4-kinases (PI4Ks), phosphatidylinositol phosphate kinases (PIPKs) [1,4] |
| Subcellular context | Golgi, plasma membrane, endosomes [1,2,3] |
| Regulatory modification | Palmitoylation of associated proteins |
| Disease relevance | Immune signaling, ciliogenesis, cancer [1,2] |
What Is GO:0005545?
1-phosphatidylinositol binding (GO:0005545) is a molecular function that describes the non-covalent interaction of a protein or protein complex with a phosphatidylinositol molecule. Phosphatidylinositol is a glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. This binding typically occurs at membrane surfaces and is mediated by specific structural domains that recognize the inositol headgroup, often in a stereospecific manner. The function is distinct from binding to phosphorylated phosphoinositides, although many proteins that bind PI also bind its phosphorylated derivatives [4,7].
Why Is 1-phosphatidylinositol binding Important in Cell Biology?
1-phosphatidylinositol binding is a fundamental molecular function that governs the recruitment and activity of lipid kinases and their effectors at specific membrane compartments. It is essential for the production of phosphoinositides, which act as signaling molecules and membrane identity determinants [4,8]. Disruption of this binding can lead to defects in Golgi-to-endosome trafficking, antiviral immunity, and ciliogenesis, highlighting its broad physiological importance [1,2]. Moreover, because many pathogens and oncogenes hijack phosphatidylinositol-binding proteins, this function is a promising target for therapeutic intervention.
• Controls the localization and activation of phosphatidylinositol 4-kinases, which are key enzymes in phosphoinositide synthesis [1,4].
• Regulates Golgi-to-endosome trafficking and STING activation in antiviral immunity.
• Mediates Rab11a activation and trafficking to promote ciliogenesis.
• Is regulated by palmitoylation, which targets calcineurin to the phosphatidylinositol 4-kinase complex at the plasma membrane.
• Influences calcium signaling through interactions with calcium-binding proteins like frequenin.
• Modulates ion channel activity, as shown for Kv7.1 binding to phosphatidylinositol 4,5-bisphosphate.
• Involved in the regulation of phosphatidylinositol 4-phosphate 5-kinase by phosphatidic acid binding.
• Dysregulation is linked to immune disorders, ciliopathies, and cancer [1,2].
• Provides a mechanism for spatial and temporal control of lipid signaling [4,8].
• Offers targets for CRISPR-based functional studies and drug discovery [1,2].
Molecular Mechanism of 1-phosphatidylinositol binding
Recognition of the Inositol Headgroup
In simple terms: Proteins bind to the inositol ring of phosphatidylinositol, like a key fitting a lock.
The binding of proteins to phosphatidylinositol involves specific recognition of the inositol headgroup, which is esterified to the sn-glycerol 3-phosphate residue. This interaction is often mediated by pleckstrin homology (PH) domains or other lipid-binding modules that form hydrogen bonds and electrostatic interactions with the inositol ring. Structural studies have shown that charge neutralization scanning can identify critical residues for phosphatidylinositol 4,5-bisphosphate binding, as demonstrated for Kv7.1. The specificity for the 1-phosphatidylinositol isomer is determined by the stereochemistry of the inositol ring and the position of the phosphate groups.
Membrane Recruitment and Complex Assembly
In simple terms: Once bound, the protein is anchored to the membrane and can assemble with other proteins.
Binding to phosphatidylinositol recruits proteins to specific membrane compartments, such as the Golgi or plasma membrane. For example, ARMH3-mediated recruitment of PI4KB to the Golgi directs Golgi-to-endosome trafficking and activation of the antiviral effector STING. Similarly, Golgi-localized PI4KB mediates Rab11a activation and trafficking to promote ciliogenesis. This recruitment often involves additional cofactors, such as palmitoylation, which targets calcineurin to the phosphatidylinositol 4-kinase complex at the plasma membrane.
Regulation by Calcium-Binding Proteins
In simple terms: Calcium sensors can interact with phosphatidylinositol-binding enzymes to modulate their activity.
Calcium-binding proteins such as frequenin (neuronal calcium sensor-1) associate productively with yeast phosphatidylinositol 4-kinase isoform Pik1, indicating that calcium signaling can regulate phosphatidylinositol binding and subsequent kinase activity. This interaction is conserved and highlights a regulatory layer where calcium levels influence lipid kinase function. Such regulation is critical for processes like secretion and membrane trafficking.
Phosphatidic Acid Modulation of PIPK Binding
In simple terms: Another lipid, phosphatidic acid, can affect how phosphatidylinositol 4-phosphate 5-kinase binds to membranes.
Phosphatidic acid binding to phosphatidylinositol 4-phosphate 5-kinase modulates its activity and localization, as reviewed by Stace et al.. This suggests that 1-phosphatidylinositol binding is not an isolated event but is influenced by the surrounding lipid environment. The interplay between phosphatidic acid and phosphatidylinositol binding may fine-tune the production of phosphatidylinositol 4,5-bisphosphate, a key signaling lipid.
Role in Phosphoinositide Synthesis
In simple terms: Binding to phosphatidylinositol is the first step in making other signaling lipids.
Phosphatidylinositol serves as a substrate for phosphatidylinositol 4-kinases and phosphatidylinositol phosphate kinases, which generate phosphorylated phosphoinositides. The binding of these enzymes to phosphatidylinositol is essential for their catalytic activity and for the spatial organization of phosphoinositide synthesis. Downes et al. described myo-inositol metabolites as cellular signals, underscoring the importance of phosphatidylinositol binding in signal transduction.
Key Genes Involved in GO:0005545 1-phosphatidylinositol binding
The following genes encode proteins that bind 1-phosphatidylinositol or are directly involved in its metabolism and downstream signaling.
| Gene | Major Role | Research Relevance |
|---|---|---|
| PI4KB | Phosphatidylinositol 4-kinase beta; binds phosphatidylinositol and phosphorylates it to PI4P | Recruited by ARMH3 to Golgi for STING activation and ciliogenesis [1,2] |
| PIK4CB | Phosphatidylinositol 4-kinase catalytic beta (alternative name for PI4KB) | Same as PI4KB [1,2] |
| ARMH3 | Mediates recruitment of PI4KB to Golgi membranes | Required for Golgi-to-endosome trafficking and STING activation |
| PIP5K1A | Phosphatidylinositol 4-phosphate 5-kinase alpha; binds phosphatidylinositol and phosphatidic acid | Regulates PI(4,5)P2 synthesis |
| PIP5K1B | Phosphatidylinositol 4-phosphate 5-kinase beta | Similar to PIP5K1A |
| PIP5K1C | Phosphatidylinositol 4-phosphate 5-kinase gamma | Involved in focal adhesion and endocytosis |
| PIK1 | Yeast phosphatidylinositol 4-kinase; binds frequenin | Model for calcium regulation of PI4K |
| FRQ1 | Yeast frequenin; calcium-binding protein that associates with Pik1 | Regulates Pik1 activity |
| KCNQ1 | Potassium channel Kv7.1; binds phosphatidylinositol 4,5-bisphosphate | Ion channel regulation by phosphoinositides |
| PPP3CA | Calcineurin A alpha; palmitoylated and targeted to PI4K complex | Links calcium signaling to PI4K regulation |
| PPP3CB | Calcineurin A beta | Similar to PPP3CA |
| PPP3R1 | Calcineurin B; regulatory subunit | Palmitoylation targets calcineurin to PI4K complex |
| STING1 | Stimulator of interferon genes; activated downstream of PI4KB | Antiviral immunity |
| RAB11A | Small GTPase; activated by PI4KB for ciliogenesis | Trafficking to cilia |
| PI4KA | Phosphatidylinositol 4-kinase alpha | Synthesizes PI4P at plasma membrane |
| PI4K2A | Phosphatidylinositol 4-kinase type 2 alpha | Endosomal PI4P synthesis |
| PI4K2B | Phosphatidylinositol 4-kinase type 2 beta | Golgi PI4P synthesis |
| NCS1 | Neuronal calcium sensor-1 (human frequenin) | Regulates PI4K signaling |
How Is 1-phosphatidylinositol binding Regulated?
1-phosphatidylinositol binding is regulated at multiple levels. Palmitoylation of calcineurin targets it to the phosphatidylinositol 4-kinase complex at the plasma membrane, thereby modulating PI4K activity. Calcium-binding proteins such as frequenin associate with yeast PI4K Pik1, linking calcium signaling to phosphatidylinositol binding. Phosphatidic acid binding to phosphatidylinositol 4-phosphate 5-kinase can influence its interaction with phosphatidylinositol and its catalytic activity. Additionally, ARMH3-mediated recruitment of PI4KB to the Golgi is a regulated step that controls downstream STING activation. These regulatory mechanisms ensure that phosphatidylinositol binding occurs at the right time and place to coordinate cellular responses.
1-phosphatidylinositol binding and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| PI4KB | Antiviral immunity, ciliogenesis | Knockout in HeLa or RPE1 cells [1,2] |
| ARMH3 | STING activation defects | Knockout in macrophages |
| KCNQ1 | Cardiac arrhythmia (Long QT syndrome) | Point mutation knock-in in cardiomyocytes |
| PIP5K1A | Cancer cell migration | Overexpression in cancer cell lines |
| PPP3CA | Neurological disorders | Knock-in of palmitoylation-deficient mutant |
Immune Signaling and Antiviral Defense
PI4KB, a phosphatidylinositol-binding enzyme, is recruited to the Golgi by ARMH3 to direct Golgi-to-endosome trafficking and activate the antiviral effector STING. Disruption of this pathway can impair innate immune responses to viral infections. Mutations in genes encoding components of this complex could lead to immunodeficiency or autoinflammatory conditions.
Ciliopathies and Developmental Disorders
Golgi-localized PI4KB mediates Rab11a activation and trafficking to promote ciliogenesis. Defects in this process can result in ciliopathies, a group of genetic disorders affecting multiple organs. Understanding how 1-phosphatidylinositol binding regulates ciliogenesis may provide insights into these diseases.
Cancer and Cell Proliferation
Phosphatidylinositol-binding proteins are often deregulated in cancer. For example, PI4KB and its product PI4P are involved in membrane trafficking pathways that support tumor growth and metastasis [1,4]. Targeting the binding interface of these proteins could offer therapeutic opportunities. However, direct evidence linking specific mutations in 1-phosphatidylinositol binding to cancer requires further study.
Neurological and Cardiac Disorders
Ion channels such as Kv7.1 bind phosphatidylinositol 4,5-bisphosphate, and mutations affecting this interaction can cause cardiac arrhythmias. Similarly, calcium-binding proteins like frequenin regulate PI4K in neurons, and their dysfunction may contribute to neurodegenerative diseases. These examples highlight the broad physiological impact of 1-phosphatidylinositol binding [5,6].
From 1-phosphatidylinositol binding-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does PI4KB binding to phosphatidylinositol regulate STING trafficking? | PI4KB knockout cells reconstituted with binding-deficient mutants |
| What is the role of ARMH3 in PI4KB recruitment? | ARMH3 knockout cells |
| How does palmitoylation affect calcineurin localization to PI4K? | Palmitoylation site mutants of calcineurin |
| Does frequenin binding to Pik1 modulate PI4K activity? | Yeast strains with FRQ1 deletion or point mutations |
| What is the impact of Kv7.1-PIP2 interaction on channel function? | KCNQ1 point mutations in heterologous expression systems |
| How does phosphatidic acid binding affect PIP5K1A activity? | PIP5K1A mutants with altered PA binding |
How to Study the 1-phosphatidylinositol binding Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Lipid overlay assay | Binding to immobilized lipids | Screening for phosphatidylinositol-binding proteins |
| Isothermal titration calorimetry | Binding affinity and stoichiometry | Quantifying protein-lipid interactions |
| Surface plasmon resonance | Real-time binding kinetics | Measuring on/off rates for phosphatidylinositol |
| Fluorescence microscopy | Subcellular localization of binding | Visualizing PI4KB recruitment to Golgi [1,2] |
| CRISPR-Cas9 knockout | Loss-of-function phenotypes | Studying ARMH3 or PI4KB function [1,2] |
| CRISPR knock-in | Effects of point mutations | Abolishing lipid binding in KCNQ1 |
| Co-immunoprecipitation | Protein-protein interactions | Identifying calcineurin-PI4K complex |
| Mass spectrometry | Protein identification and modifications | Detecting palmitoylation of calcineurin |
Lipid Overlay and Binding Assays
Lipid overlay assays using membrane strips spotted with various phospholipids can identify proteins that bind specifically to phosphatidylinositol. This method is useful for screening candidate proteins and for mapping binding domains [4,7]. Isothermal titration calorimetry (ITC) and surface plasmon resonance (SPR) can provide quantitative binding affinities.
Fluorescence Microscopy and Live-Cell Imaging
GFP-tagged lipid-binding domains or fluorescently labeled phosphatidylinositol analogs can be used to visualize binding in live cells. For example, the recruitment of PI4KB to the Golgi can be monitored by confocal microscopy [1,2]. Total internal reflection fluorescence (TIRF) microscopy can resolve binding events at the plasma membrane.
CRISPR-Cas9 Knockout and Knock-in
CRISPR-Cas9 can generate knockout cell lines for genes encoding phosphatidylinositol-binding proteins, such as PI4KB or ARMH3, to study loss-of-function phenotypes [1,2]. Knock-in of point mutations that abolish lipid binding can dissect the specific contribution of 1-phosphatidylinositol binding to protein function.
Proteomics and Interactomics
Affinity purification coupled with mass spectrometry can identify proteins that co-purify with phosphatidylinositol or its binding proteins. This approach can reveal novel components of the phosphatidylinositol-binding complex and their post-translational modifications [3,5].
How CRISPR Can Be Used to Study GO:0005545 1-phosphatidylinositol binding
Knockout
CRISPR-Cas9 knockout of genes encoding phosphatidylinositol-binding proteins, such as PI4KB or ARMH3, can reveal their essential roles in cellular processes. For example, PI4KB knockout impairs Golgi-to-endosome trafficking and STING activation. Similarly, ARMH3 knockout prevents PI4KB recruitment to the Golgi. These models are valuable for studying loss-of-function phenotypes and for validating drug targets.
Point Mutation
Introducing point mutations that specifically abolish phosphatidylinositol binding without affecting protein stability or other functions can dissect the contribution of this binding to protein activity. For instance, charge neutralization scanning of Kv7.1 identified residues critical for PIP2 binding. Such point mutants can be knocked into the endogenous locus using CRISPR-Cas9 to study physiological consequences.
Knock-in
Knock-in of tagged versions of phosphatidylinositol-binding proteins, such as GFP or HA tags, allows for real-time imaging and biochemical purification. This approach has been used to study the localization of PI4KB at the Golgi [1,2]. Knock-in of disease-associated mutations can also model human disorders, such as cardiac arrhythmias linked to KCNQ1 mutations.
Overexpression
Overexpression of wild-type or mutant phosphatidylinositol-binding proteins can be achieved by CRISPR activation (CRISPRa) or by lentiviral transduction. Overexpression of PIP5K1A, for example, can increase phosphatidylinositol 4,5-bisphosphate levels and affect cell migration. This approach is useful for gain-of-function studies and for identifying downstream effects.
How EDITGENE Supports 1-phosphatidylinositol binding Research
Researchers studying 1-phosphatidylinositol binding-related genes often need to determine whether a candidate gene is causally involved in a specific cellular process or disease. This requires precise genetic models that can isolate the contribution of lipid binding from other protein functions. EDITGENE provides a comprehensive suite of CRISPR services to generate such models efficiently and reliably.
Contact EDITGENE today to design your custom CRISPR model for 1-phosphatidylinositol binding research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| ZFYVE16 Knockout HEK293 Cell Line | EDJ-KQ411 | Human | 9765 | Details Get a Quote |
| ZFYVE9 Knockout HEK293 Cell Line | EDJ-KQ412 | Human | 9372 | Details Get a Quote |
| SCARB1 Knockout HEK293 Cell Line | EDJ-KQ2450 | Human | 949 | Details Get a Quote |
| SNX9 Knockout HEK293 Cell Line | EDJ-KQ3063 | Human | 51429 | Details Get a Quote |
| EEA1 Knockout HEK293 Cell Line | EDJ-KQ3219 | Human | 8411 | Details Get a Quote |
| EPB41 Knockout HEK293 Cell Line | EDJ-KQ4541 | Human | 2035 | Details Get a Quote |
| SNAP91 Knockout HEK293 Cell Line | EDJ-KQ6806 | Human | 9892 | Details Get a Quote |
| WDFY3 Knockout HEK293 Cell Line | EDJ-KQ7770 | Human | 23001 | Details Get a Quote |
| SNX10 Knockout HEK293 Cell Line | EDJ-KQ9063 | Human | 29887 | Details Get a Quote |
| FRMPD2 Knockout HEK293 Cell Line | EDJ-KQ10315 | Human | 143162 | Details Get a Quote |
| SCIN Knockout HEK293 Cell Line | EDJ-KQ10378 | Human | 85477 | Details Get a Quote |
| SESTD1 Knockout HEK293 Cell Line | EDJ-KQ10730 | Human | 91404 | Details Get a Quote |
| PICALM Knockout HEK293 Cell Line | EDJ-KQ14752 | Human | 8301 | Details Get a Quote |
| WDFY1 Knockout HEK293 Cell Line | EDJ-KQ15347 | Human | 57590 | Details Get a Quote |
| ZFYVE9 Knockout HeLa Cell Line | EDJ-KQ17994 | Human | 9372 | Details Get a Quote |
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Frequently Asked Questions About 1-phosphatidylinositol binding
What is 1-phosphatidylinositol binding?
1-phosphatidylinositol binding (GO:0005545) is a molecular function where a protein binds to phosphatidylinositol, a glycophospholipid with its sn-glycerol 3-phosphate residue esterified to the 1-hydroxyl group of 1D-myo-inositol.
What genes are involved in 1-phosphatidylinositol binding?
Genes encoding phosphatidylinositol 4-kinases (PI4KB, PI4KA), phosphatidylinositol phosphate kinases (PIP5K1A, PIP5K1B, PIP5K1C), and regulatory proteins like ARMH3 and calcineurin (PPP3CA) are involved [1,3,4,7].
How does 1-phosphatidylinositol binding regulate STING activation?
PI4KB is recruited to the Golgi by ARMH3, where it binds phosphatidylinositol and directs Golgi-to-endosome trafficking to activate STING.
What is the role of PI4KB in ciliogenesis?
Golgi-localized PI4KB binds phosphatidylinositol and mediates Rab11a activation and trafficking to promote ciliogenesis.
How is 1-phosphatidylinositol binding regulated by palmitoylation?
Palmitoylation targets calcineurin to the phosphatidylinositol 4-kinase complex at the plasma membrane, thereby regulating PI4K activity.
Which diseases are associated with defects in 1-phosphatidylinositol binding?
Defects are linked to impaired antiviral immunity, ciliopathies, cardiac arrhythmias, and cancer [1,2,6].
What methods are used to study 1-phosphatidylinositol binding?
Common methods include lipid overlay assays, isothermal titration calorimetry, fluorescence microscopy, CRISPR knockout/knock-in, and proteomics [1,4,6].
Can CRISPR be used to study 1-phosphatidylinositol binding?
Yes, CRISPR-Cas9 can generate knockouts, point mutations, and knock-ins to dissect the function of phosphatidylinositol-binding proteins [1,2,6].
What is the difference between 1-phosphatidylinositol binding and PIP2 binding?
1-phosphatidylinositol binding refers to binding the unphosphorylated lipid, while PIP2 binding involves phosphorylated derivatives; many proteins bind both but with different affinities [4,6].
How does calcium signaling affect 1-phosphatidylinositol binding?
Calcium-binding proteins like frequenin associate with phosphatidylinositol 4-kinases, modulating their activity and localization.
Conclusion
1-phosphatidylinositol binding (GO:0005545) is a fundamental molecular function that orchestrates membrane recruitment and activation of lipid kinases and their effectors. Its roles in Golgi-to-endosome trafficking, STING activation, ciliogenesis, and ion channel regulation underscore its broad physiological importance [1,2,6]. Dysregulation of this function contributes to immune disorders, ciliopathies, and cancer, making it a compelling target for therapeutic development [1,2]. Advances in CRISPR-based models and lipid-binding assays will continue to illuminate the mechanistic details and disease relevance of 1-phosphatidylinositol binding.
References
- 1. Fang R et al.. 2023. ARMH3-mediated recruitment of PI4KB directs Golgi-to-endosome trafficking and activation of the antiviral effector STING.. Immunity 56(3):500-515.e6 PMID: 36921576
- 2. Wang L et al.. 2025. Golgi-localized phosphatidylinositol 4-kinase β mediates Rab11a activation and trafficking to promote ciliogenesis.. Sci Adv 11(49):eadw6910 PMID: 41348894
- 3. Ulengin-Talkish I et al.. 2021. Palmitoylation targets the calcineurin phosphatase to the phosphatidylinositol 4-kinase complex at the plasma membrane.. Nat Commun 12(1):6064 PMID: 34663815
- 4. Giudici ML et al.. 2004. Phosphatidylinositol phosphate kinases.. J Endocrinol Invest 27(6 Suppl):137-42 PMID: 15481814
- 5. Strahl T et al.. 2003. Conservation of regulatory function in calcium-binding proteins: human frequenin (neuronal calcium sensor-1) associates productively with yeast phosphatidylinositol 4-kinase isoform, Pik1.. J Biol Chem 278(49):49589-99 PMID: 14512421
- 6. Eckey K et al.. 2014. Novel Kv7.1-phosphatidylinositol 4,5-bisphosphate interaction sites uncovered by charge neutralization scanning.. J Biol Chem 289(33):22749-22758 PMID: 24947509
- 7. Stace C et al.. 2008. PA binding of phosphatidylinositol 4-phosphate 5-kinase.. Adv Enzyme Regul 48:55-72 PMID: 18167315
- 8. Downes CP et al.. 1990. myo-inositol metabolites as cellular signals.. Eur J Biochem 193(1):1-18 PMID: 2171926
