GO:0052827 inositol pentakisphosphate phosphatase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0052827 describes the catalytic removal of a phosphate group from myo-inositol pentakisphosphate to yield myo-inositol tetrakisphosphate and free phosphate.
• This activity is carried out by multiple inositol polyphosphate phosphatases, including MINPP1 and PTEN, which act on distinct inositol pentakisphosphate isomers [4,7].
• The reaction is part of the inositol polyphosphate signaling network that regulates calcium mobilization, vesicular trafficking, and gene expression [1,2].
• Loss of inositol pentakisphosphate phosphatase activity has been linked to cancer progression and developmental defects in model organisms [4,7].
• Studying this activity requires precise assays that distinguish between different inositol phosphate isomers and phosphatase classes [3,6].
• CRISPR-based knockout, point-mutation, and knock-in models are essential to dissect the physiological roles of these phosphatases [4,7].
Description
Inositol polyphosphates are a family of soluble signaling molecules that control diverse cellular processes, including calcium signaling, membrane trafficking, and chromatin remodeling [1,2]. The enzyme activity defined by GO:0052827, inositol pentakisphosphate phosphatase activity, specifically catalyzes the hydrolysis of myo-inositol pentakisphosphate to myo-inositol tetrakisphosphate and inorganic phosphate. This reaction is a key step in the metabolic interconversion of inositol polyphosphates and helps set the cellular levels of these important second messengers. Researchers study this activity to understand how cells terminate or modulate inositol phosphate signals and how dysregulation contributes to disease [4,7]. The activity is mediated by several distinct enzymes, including multiple inositol polyphosphate phosphatase (MINPP1) and the tumor suppressor PTEN, which exhibit overlapping but distinct substrate specificities [4,7]. Because different inositol pentakisphosphate isomers exist, the precise positional specificity of each phosphatase is critical for its biological function [1,3]. This article provides a comprehensive overview of the molecular mechanism, key genes, disease relevance, and experimental approaches for studying GO:0052827.
inositol pentakisphosphate phosphatase activity At A Glance
| GO ID | GO:0052827 |
|---|---|
| GO term | inositol pentakisphosphate phosphatase activity |
| Ontology | molecular_function |
| Synonym | none |
| Definition | Catalysis of the reaction: myo-inositol pentakisphosphate + H2O = myo-inositol tetrakisphosphate + phosphate. |
| Major function | Hydrolysis of a phosphate group from inositol pentakisphosphate, regulating inositol polyphosphate signaling. |
| Representative enzymes | MINPP1, PTEN, and other multiple inositol polyphosphate phosphatases [4,7]. |
| Substrate specificity | Acts on various inositol pentakisphosphate isomers, including Ins(1,3,4,5,6)P5 and Ins(1,2,3,4,6)P5 [1,3]. |
| Biological context | Inositol polyphosphate metabolism, calcium signaling, and cell growth control [1,2]. |
What Is GO:0052827?
GO:0052827, inositol pentakisphosphate phosphatase activity, is a molecular function defined as the catalysis of the reaction: myo-inositol pentakisphosphate + H2O = myo-inositol tetrakisphosphate + phosphate. In other words, it is the enzymatic removal of a phosphate group from an inositol pentakisphosphate molecule, producing an inositol tetrakisphosphate and free phosphate. This activity is part of the broader class of inositol polyphosphate phosphatases and is distinguished by its substrate specificity for pentakisphosphates rather than other inositol phosphates [1,3].
Why Is inositol pentakisphosphate phosphatase activity Important in Cell Biology?
Inositol pentakisphosphate phosphatase activity is important because it directly controls the cellular levels of inositol pentakisphosphates and tetrakisphosphates, which are key signaling molecules involved in calcium mobilization, vesicular trafficking, and gene expression [1,2]. By removing a phosphate group, this activity can terminate or modulate signals that would otherwise be mediated by these inositol polyphosphates. Dysregulation of this activity has been implicated in cancer, as PTEN, a well-known tumor suppressor, possesses inositol pentakisphosphate 3-phosphatase activity. Additionally, MINPP1, another enzyme with this activity, is critical for normal development and has been linked to developmental defects in knockout mice. Therefore, understanding GO:0052827 is essential for deciphering the complex signaling networks that govern cell behavior and for developing therapeutic strategies targeting these pathways.
• Regulates the levels of inositol pentakisphosphates and tetrakisphosphates, which are important second messengers [1,2].
• Contributes to calcium signaling and membrane trafficking by controlling inositol polyphosphate pools.
• The tumor suppressor PTEN exhibits inositol pentakisphosphate 3-phosphatase activity, linking this activity to cancer suppression.
• MINPP1 knockout mice display developmental defects, highlighting the physiological importance of this activity.
• Inositol polyphosphates are involved in chromatin remodeling and gene expression, so this activity can influence transcription.
• Altered inositol phosphate metabolism has been observed in T-cell activation, suggesting a role in immune responses.
• This activity is a potential target for therapeutic intervention in diseases with dysregulated inositol signaling.
• Studying this activity helps distinguish between different inositol phosphate phosphatases and their specific roles.
• Plant phosphoinositide-dependent phospholipases C and related enzymes may also possess this activity, indicating evolutionary conservation.
• Understanding substrate specificity of this activity is crucial for designing selective inhibitors [5,6].
Molecular Mechanism of inositol pentakisphosphate phosphatase activity
Substrate recognition and binding
In simple terms: The enzyme grabs a specific inositol pentakisphosphate molecule from the surrounding fluid.
Inositol pentakisphosphate phosphatases recognize their substrates through a conserved active site that accommodates the inositol ring and its phosphate groups. Different enzymes exhibit specificity for distinct isomers, such as D-myo-inositol 1,2,3,4,6-pentakisphosphate or D-myo-inositol 1,3,4,5,6-pentakisphosphate. The binding is mediated by electrostatic interactions between positively charged residues in the active site and the negatively charged phosphate groups of the substrate. This initial recognition ensures that only the correct inositol pentakisphosphate is processed, preventing wasteful hydrolysis of other inositol phosphates.
Catalytic hydrolysis of the phosphate group
In simple terms: The enzyme uses water to cut off one phosphate group from the inositol ring.
Once bound, the enzyme catalyzes the hydrolysis of the phosphomonoester bond, releasing inorganic phosphate and producing an inositol tetrakisphosphate. This reaction typically involves a nucleophilic water molecule activated by a metal ion or an amino acid residue in the active site. The specific position of the phosphate removed depends on the enzyme; for example, a D-myo-inositol 1,2,3,4,6-pentakisphosphate-2-phosphomonoesterase removes the phosphate at the 2-position, while a D-myo-inositol 1,3,4,5,6-pentakisphosphate-1/3-phosphatase acts at the 1 or 3 position. The reaction is energetically favorable and essentially irreversible under physiological conditions.
Product release and conformational changes
In simple terms: After cutting the phosphate, the enzyme lets go of the products and resets for another round.
Following hydrolysis, the inositol tetrakisphosphate and phosphate products are released from the active site. This step may involve conformational changes that weaken product binding and allow the enzyme to return to its resting state. Some enzymes, such as PTEN, can process multiple inositol phosphate substrates, and product release may be a regulated step. The released inositol tetrakisphosphate can then participate in further signaling or metabolic pathways.
Regulation by cellular factors
In simple terms: Other molecules in the cell can speed up or slow down the enzyme.
The activity of inositol pentakisphosphate phosphatases can be modulated by various cellular factors. For instance, inositol 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate inhibit inositol-1,3,4,5-tetrakisphosphate 3-phosphatase in rat parotid glands, indicating feedback regulation. Vicinal thiols are involved in the activity of inositol 1,2,3,5,6-pentakisphosphate 5-phosphatase from fetal calf thymus, suggesting redox sensitivity. Additionally, the activity of PTEN can be regulated by its lipid phosphatase activity and protein interactions.
Isoform diversity and substrate specificity
In simple terms: Different versions of the enzyme prefer different inositol pentakisphosphate shapes.
Multiple enzymes exhibit inositol pentakisphosphate phosphatase activity, each with distinct substrate preferences. MINPP1 is a multiple inositol polyphosphate phosphatase that can act on various inositol phosphates, including pentakisphosphates. PTEN, primarily known as a lipid phosphatase, also possesses inositol 1,3,4,5,6-pentakisphosphate 3-phosphatase activity. Other activities, such as D-myo-inositol 1,2,3,4,6-pentakisphosphate-2-phosphomonoesterase and D-myo-inositol 1,3,4,5,6-pentakisphosphate-1/3-phosphatase, have been identified in T-lymphocytes. This diversity allows for fine-tuned regulation of different inositol phosphate pools.
Key Genes Involved in GO:0052827 inositol pentakisphosphate phosphatase activity
The following genes encode enzymes that possess inositol pentakisphosphate phosphatase activity or are directly involved in its regulation, as supported by published literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| MINPP1 | Multiple inositol polyphosphate phosphatase; hydrolyzes various inositol phosphates including pentakisphosphates. | Knockout mice reveal developmental roles; potential tumor suppressor. |
| PTEN | Lipid and protein phosphatase; exhibits inositol 1,3,4,5,6-pentakisphosphate 3-phosphatase activity. | Major tumor suppressor; mutations linked to cancer. |
| INPP5A | Inositol polyphosphate 5-phosphatase; may act on pentakisphosphates. | Studied for its role in calcium signaling and cancer. |
| INPP5B | Inositol polyphosphate 5-phosphatase; potential activity on inositol pentakisphosphates. | Involved in vesicular trafficking and signaling. |
| INPPL1 | Inositol polyphosphate phosphatase-like 1; may dephosphorylate inositol pentakisphosphates. | Linked to insulin signaling and cytoskeletal regulation. |
| SYNJ1 | Synaptojanin 1; polyphosphoinositide phosphatase with potential inositol pentakisphosphate activity. | Implicated in synaptic vesicle recycling and Parkinson's disease. |
| SYNJ2 | Synaptojanin 2; similar to SYNJ1, may act on inositol pentakisphosphates. | Role in cell migration and cancer. |
| OCRL | Oculocerebrorenal syndrome of Lowe protein; inositol polyphosphate 5-phosphatase. | Mutations cause Lowe syndrome; may affect inositol phosphate metabolism. |
| INPP4A | Inositol polyphosphate 4-phosphatase; may indirectly influence pentakisphosphate levels. | Associated with neurological disorders. |
| INPP4B | Inositol polyphosphate 4-phosphatase type II; potential role in pentakisphosphate metabolism. | Tumor suppressor in breast cancer. |
| ITPK1 | Inositol-tetrakisphosphate 1-kinase; synthesizes inositol pentakisphosphates, opposing phosphatase activity. | Regulates inositol phosphate pools; involved in development. |
| IPPK | Inositol-pentakisphosphate 2-kinase; converts pentakisphosphate to hexakisphosphate. | Affects inositol pyrophosphate synthesis. |
| PPIP5K1 | Diphosphoinositol pentakisphosphate kinase; regulates inositol pyrophosphates. | Linked to energy metabolism and cancer. |
| PPIP5K2 | Diphosphoinositol pentakisphosphate kinase 2; similar to PPIP5K1. | Potential role in cell signaling. |
| PLCβ1 | Phospholipase C beta 1; generates inositol phosphates including pentakisphosphates. | Plant homologs studied for stress responses. |
| PLCγ1 | Phospholipase C gamma 1; produces inositol polyphosphates. | Involved in immune signaling and cancer. |
| PLCD1 | Phospholipase C delta 1; contributes to inositol phosphate pool. | Role in hair follicle and skin development. |
| PLCE1 | Phospholipase C epsilon 1; regulates inositol phosphate signaling. | Implicated in cancer and kidney disease. |
How Is inositol pentakisphosphate phosphatase activity Regulated?
The activity of inositol pentakisphosphate phosphatases is regulated at multiple levels. Substrate availability and product inhibition play key roles; for example, inositol 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate inhibit inositol-1,3,4,5-tetrakisphosphate 3-phosphatase in rat parotid glands. Redox state can modulate activity, as vicinal thiols are involved in inositol 1,2,3,5,6-pentakisphosphate 5-phosphatase from fetal calf thymus. PTEN activity is regulated by its own phosphorylation, ubiquitination, and interactions with membrane lipids. Additionally, the expression levels of these enzymes are controlled transcriptionally and post-translationally, allowing cells to adapt to changing signaling demands.
inositol pentakisphosphate phosphatase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| PTEN | Cancer (multiple types), tumor suppression | Knockout and point-mutation cell lines; xenograft models |
| MINPP1 | Developmental defects, skeletal abnormalities | Minpp1 knockout mice; CRISPR knockout in cell lines |
| SYNJ1 | Parkinson's disease, synaptic dysfunction | Knock-in of patient mutations; neuronal cultures |
| OCRL | Lowe syndrome, developmental disorder | Patient-derived fibroblasts; knockout models |
| INPP5A | Cancer, calcium signaling | Overexpression and knockout cell lines |
Cancer
PTEN is one of the most frequently mutated tumor suppressors in human cancers, and its inositol 1,3,4,5,6-pentakisphosphate 3-phosphatase activity contributes to its tumor-suppressive functions. Loss of PTEN leads to accumulation of inositol pentakisphosphates, which can promote cell survival and proliferation. MINPP1, another enzyme with this activity, has been implicated in cancer through its role in inositol phosphate metabolism. Targeting inositol pentakisphosphate phosphatases may offer therapeutic opportunities in cancers with dysregulated inositol signaling.
Developmental disorders
Targeted deletion of Minpp1 in mice provides insight into the activity of multiple inositol polyphosphate phosphatase in vivo, revealing its importance in development. MINPP1 knockout mice exhibit growth retardation and skeletal abnormalities, suggesting that inositol pentakisphosphate phosphatase activity is critical for normal development. Mutations in genes encoding inositol polyphosphate phosphatases, such as OCRL, cause Lowe syndrome, a developmental disorder affecting the eyes, brain, and kidneys.
Neurological disorders
Synaptojanin 1 (SYNJ1) is a polyphosphoinositide phosphatase that may also act on inositol pentakisphosphates, and mutations in SYNJ1 have been linked to early-onset Parkinson's disease. Dysregulation of inositol phosphate signaling in neurons can impair synaptic vesicle recycling and contribute to neurodegeneration. Additionally, inositol polyphosphates are involved in calcium signaling, which is critical for neuronal function.
Immune dysfunction
T-cell receptor-mediated metabolism of inositol polyphosphates in Jurkat T-lymphocytes identifies specific inositol pentakisphosphate phosphatase activities, indicating a role in immune cell activation. Proper regulation of these activities is necessary for normal immune responses, and their dysregulation may contribute to autoimmune diseases or immunodeficiency.
From inositol pentakisphosphate phosphatase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of MINPP1 affect inositol pentakisphosphate levels? | MINPP1 knockout cell line (CRISPR-Cas9) |
| How does a specific point mutation in PTEN affect its inositol pentakisphosphate phosphatase activity? | PTEN point-mutation knock-in cell line |
| What is the subcellular localization of inositol pentakisphosphate phosphatases? | Tagged knock-in (e.g., GFP) cell line |
| Does overexpression of INPP5A alter calcium signaling? | INPP5A overexpression cell line |
| Which genes are synthetic lethal with PTEN loss? | CRISPR library screening in PTEN-null cells |
| Can we identify small molecule inhibitors of MINPP1? | High-throughput screening with purified enzyme or cell-based assays |
How to Study the inositol pentakisphosphate phosphatase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| HPLC/TLC enzymatic assay | Phosphatase activity and substrate specificity | Purified enzyme characterization |
| CRISPR-Cas9 knockout | Loss-of-function phenotypes | Gene function studies in cell lines |
| CRISPR point mutation | Effect of catalytic inactivation | Dissecting enzyme activity from scaffolding functions |
| Mass spectrometry | Inositol phosphate levels | Metabolic profiling of mutant cells |
| Fluorescent biosensors | Real-time signaling dynamics | Live-cell imaging of calcium and inositol phosphates |
| RNA-seq | Transcriptional changes upon enzyme loss | Identifying downstream pathways |
| Proteomics | Protein interactions and post-translational modifications | Mapping signaling complexes |
| CRISPR library screening | Synthetic lethal interactions | Identifying therapeutic targets in cancer |
Enzymatic assays for phosphatase activity
Direct measurement of inositol pentakisphosphate phosphatase activity typically involves incubating the enzyme with radiolabeled or fluorescently labeled inositol pentakisphosphate substrates and separating products by chromatography [1,3]. High-performance liquid chromatography (HPLC) or thin-layer chromatography (TLC) can resolve different inositol phosphate isomers, allowing determination of substrate specificity and kinetic parameters. These assays are essential for validating the activity of purified enzymes or cell lysates.
Genetic manipulation with CRISPR-Cas9
CRISPR-Cas9 technology enables the generation of knockout, point-mutation, and knock-in cell models to study the physiological roles of inositol pentakisphosphate phosphatases [4,7]. Knockout models eliminate enzyme expression, while point mutations can abrogate catalytic activity without affecting protein stability. Knock-in of tagged versions allows for localization and interaction studies. These models are crucial for linking specific activities to cellular phenotypes.
Mass spectrometry-based inositol phosphate profiling
Mass spectrometry (MS) can quantify inositol polyphosphates in biological samples with high sensitivity and specificity. By comparing wild-type and mutant cells, researchers can determine how loss of a specific phosphatase affects the levels of inositol pentakisphosphates and tetrakisphosphates. This approach provides a global view of inositol phosphate metabolism and can reveal compensatory changes.
Live-cell imaging of signaling dynamics
Genetically encoded fluorescent biosensors for inositol polyphosphates or calcium can be used to monitor real-time signaling in live cells. Combining these sensors with CRISPR-engineered cells lacking specific phosphatases allows researchers to observe how the activity of GO:0052827 shapes signaling kinetics. This method is particularly useful for studying rapid signaling events in immune cells or neurons.
How CRISPR Can Be Used to Study GO:0052827 inositol pentakisphosphate phosphatase activity
Knockout
CRISPR-Cas9 knockout of genes encoding inositol pentakisphosphate phosphatases, such as MINPP1 or PTEN, allows researchers to study the consequences of losing this activity entirely [4,7]. Knockout cell lines can be used to measure changes in inositol phosphate levels, signaling pathways, and cellular phenotypes like proliferation or migration. These models are foundational for understanding the physiological roles of GO:0052827.
Point Mutation
Point mutations that specifically abolish catalytic activity without affecting protein expression or interactions are valuable for dissecting the precise contribution of inositol pentakisphosphate phosphatase activity. For example, a catalytically dead PTEN mutant can distinguish between its lipid phosphatase and inositol pentakisphosphate phosphatase functions. Such models are generated by CRISPR-Cas9-mediated homology-directed repair.
Knock-in
Knock-in of epitope tags (e.g., FLAG, GFP) or fluorescent proteins into endogenous loci enables visualization and immunoprecipitation of inositol pentakisphosphate phosphatases at physiological expression levels. Tagged knock-in models are useful for studying subcellular localization, protein interactions, and real-time dynamics. They can also be combined with live-cell imaging to track enzyme movement.
Overexpression
Overexpression of wild-type or mutant inositol pentakisphosphate phosphatases using CRISPR activation or lentiviral vectors can reveal gain-of-function phenotypes and help identify downstream effectors. Overexpression models are particularly useful for testing whether increased activity is sufficient to drive specific cellular outcomes, such as reduced proliferation or altered signaling.
How EDITGENE Supports inositol pentakisphosphate phosphatase activity Research
Researchers studying inositol pentakisphosphate phosphatase activity-related genes often need to determine whether a candidate gene is causally involved in a specific signaling pathway or disease phenotype. EDITGENE provides a comprehensive suite of CRISPR-based services to generate precisely engineered cell models, enabling rigorous functional studies of GO:0052827 and its associated genes.
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Frequently Asked Questions About inositol pentakisphosphate phosphatase activity
What is inositol pentakisphosphate phosphatase activity?
It is the enzymatic activity defined by GO:0052827 that removes a phosphate group from myo-inositol pentakisphosphate to produce myo-inositol tetrakisphosphate and phosphate.
What genes are involved in inositol pentakisphosphate phosphatase activity?
Key genes include MINPP1, PTEN, INPP5A, and other inositol polyphosphate phosphatases [4,7].
What is the reaction catalyzed by GO:0052827?
The reaction is: myo-inositol pentakisphosphate + H2O = myo-inositol tetrakisphosphate + phosphate.
How is inositol pentakisphosphate phosphatase activity regulated?
It is regulated by substrate availability, product inhibition, redox state, and post-translational modifications of the enzymes [2,6].
Which diseases are associated with inositol pentakisphosphate phosphatase activity?
Cancer, developmental disorders, neurological disorders, and immune dysfunction have been linked to dysregulation of this activity [4,7].
What methods are used to study inositol pentakisphosphate phosphatase activity?
Common methods include enzymatic assays with radiolabeled substrates, HPLC, mass spectrometry, and CRISPR-based genetic models [1,3].
How can CRISPR be used to study GO:0052827?
CRISPR can generate knockout, point-mutation, and knock-in cell models to dissect the physiological roles of inositol pentakisphosphate phosphatases [4,7].
What is the substrate specificity of inositol pentakisphosphate phosphatases?
Different enzymes act on specific isomers, such as Ins(1,3,4,5,6)P5 or Ins(1,2,3,4,6)P5, at distinct phosphate positions [1,3].
Is PTEN an inositol pentakisphosphate phosphatase?
Yes, PTEN exhibits inositol 1,3,4,5,6-pentakisphosphate 3-phosphatase activity in addition to its lipid phosphatase activity.
What are the potential therapeutic implications of targeting this activity?
Inhibiting or activating specific inositol pentakisphosphate phosphatases could modulate signaling pathways in cancer and other diseases.
Conclusion
Inositol pentakisphosphate phosphatase activity (GO:0052827) is a critical enzymatic function that regulates the levels of inositol polyphosphate second messengers. Through the action of enzymes like MINPP1 and PTEN, this activity influences diverse cellular processes, including calcium signaling, development, and tumor suppression [4,7]. Understanding its molecular mechanism and regulation provides insights into human diseases and potential therapeutic targets. CRISPR-based models are indispensable tools for dissecting the specific roles of these phosphatases in health and disease [4,7].
References
- 1. Guse AH et al.. 1991. T-cell receptor-mediated metabolism of inositol polyphosphates in Jurkat T-lymphocytes. Identification of a D-myo-inositol 1,2,3,4,6-pentakisphosphate-2-phosphomonoesterase activity, a D-myo-inositol 1,3,4,5,6-pentakisphosphate-1/3-phosphatase activity and a D/L-myo-inositol 1,2,4,5,6-pentakisphosphate-1/3-kinase activity.. J Biol Chem 266(36):24498-502 PMID: 1662211
- 2. Hughes PJ et al.. 1990. Inositol 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate inhibit inositol-1,3,4,5-tetrakisphosphate 3-phosphatase in rat parotid glands.. J Biol Chem 265(17):9869-75 PMID: 2161845
- 3. Nogimori K et al.. 1991. Purification of an inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase activity from rat liver and the evaluation of its substrate specificity.. J Biol Chem 266(25):16499-506 PMID: 1653239
- 4. Chi H et al.. 2000. Targeted deletion of Minpp1 provides new insight into the activity of multiple inositol polyphosphate phosphatase in vivo.. Mol Cell Biol 20(17):6496-507 PMID: 10938126
- 5. Riley AM et al.. 2006. scyllo-inositol pentakisphosphate as an analogue of myo-inositol 1,3,4,5,6-pentakisphosphate: chemical synthesis, physicochemistry and biological applications.. Chembiochem 7(7):1114-22 PMID: 16755629
- 6. Bandyopadhyay U et al.. 1997. Vicinal thiols are involved in inositol 1,2,3,5,6-pentakisphosphate 5-phosphatase activity from fetal calf thymus.. Biochem Biophys Res Commun 240(1):146-9 PMID: 9367900
- 7. Caffrey JJ et al.. 2001. Expanding coincident signaling by PTEN through its inositol 1,3,4,5,6-pentakisphosphate 3-phosphatase activity.. FEBS Lett 499(1-2):6-10 PMID: 11418101
- 8. Pokotylo I et al.. 2014. Plant phosphoinositide-dependent phospholipases C: variations around a canonical theme.. Biochimie 96:144-57 PMID: 23856562
