GO:0004445 inositol-polyphosphate 5-phosphatase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0004445 describes the enzymatic activity that removes the 5-phosphate from inositol polyphosphates such as Ins(1,4,5)P3 and Ins(1,3,4,5)P4, thereby terminating or reshaping calcium and lipid signaling.
• The reaction catalyzed is D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate, and 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
• Proteins carrying this activity include SHIP1, SHIP2, INPP5K, PIPP, and several plant and parasite 5-phosphatases, many of which are regulated by modular domains such as C2, SH2, and proline-rich regions.
• Loss or gain of 5-phosphatase activity alters phosphoinositide 3-kinase (PI3K) signaling, actin remodeling, axon outgrowth, and immune cell activation, linking the term to cancer, neurodevelopmental disorders, and metabolic disease.
• CRISPR knockout, point-mutation, knock-in, and overexpression models are the primary tools for testing causality of specific 5-phosphatase genes in these pathways.
• Researchers can measure 5-phosphatase activity with radioactive or fluorescent inositol phosphate substrates, phosphoinositide profiling, and downstream signaling readouts such as Akt phosphorylation.
Description
Inositol-polyphosphate 5-phosphatase activity (GO:0004445) is a molecular function that hydrolyzes the 5-position phosphate from inositol polyphosphates, including D-myo-inositol 1,4,5-trisphosphate and 1D-myo-inositol 1,3,4,5-tetrakisphosphate. This activity is central to phosphoinositide signaling because it converts soluble inositol polyphosphates into products that no longer mobilize calcium or recruit effector proteins, thereby shaping the amplitude and duration of second-messenger signals. The same catalytic activity also acts on lipid substrates such as phosphatidylinositol 3,4,5-trisphosphate in some enzymes, connecting GO:0004445 to PI3K-dependent pathways that control cell growth, survival, and motility. Researchers study GO:0004445 because dysregulated inositol polyphosphate 5-phosphatases contribute to cancer, immune dysfunction, and neurological disease. For example, SHIP1 and SHIP2 are well-characterized 5-phosphatases whose C2 domains regulate catalytic activity and substrate access, and mutations in these proteins alter hematopoietic and metabolic signaling. INPP5K, another 5-phosphatase, promotes corticospinal tract axon sprouting after central nervous system trauma, indicating roles in neural repair. Plant and parasite 5-phosphatases such as Gs5PTase8 from wild soybean have also been expressed and purified to study their enzymatic properties, showing the broad conservation of this activity. From a methods perspective, GO:0004445 is interrogated with biochemical assays using radiolabeled or fluorescent inositol phosphate substrates, phosphoinositide lipid profiling, and genetic perturbation of the encoding genes. Because the activity is often embedded in multidomain proteins, domain-deletion and point-mutation studies are needed to separate catalytic contributions from regulatory module functions. This article summarizes the definition, mechanism, key genes, disease links, and experimental models for GO:0004445, with all factual statements tied to verified PubMed citations.
inositol-polyphosphate 5-phosphatase activity At A Glance
| GO ID | GO:0004445 |
|---|---|
| GO term | inositol-polyphosphate 5-phosphatase activity |
| Ontology | molecular_function |
| Synonym | Ins(1,4,5)P3 5-phosphatase activity; 5PTase activity; inositol polyphosphate-5-phosphatase activity; type I inositol-polyphosphate phosphatase activity; type II inositol-1,4,5-trisphosphate 5-phosphatase activity |
| Major function | Hydrolyzes the 5-phosphate from inositol polyphosphates such as Ins(1,4,5)P3 and Ins(1,3,4,5)P4, terminating or modulating second-messenger signaling. |
| Substrates | D-myo-inositol 1,4,5-trisphosphate; 1D-myo-inositol 1,3,4,5-tetrakisphosphate; some enzymes also act on phosphatidylinositol 3,4,5-trisphosphate. |
| Products | myo-inositol 1,4-bisphosphate and phosphate; 1D-myo-inositol 1,3,4-trisphosphate and phosphate. |
| Representative enzymes | SHIP1 (INPP5D), SHIP2 (INPPL1), INPP5K, PIPP (INPP5J), Gs5PTase8. |
| Regulatory domains | C2, SH2, proline-rich, and catalytic 5-phosphatase domains modulate activity and localization. |
What Is GO:0004445?
GO:0004445, inositol-polyphosphate 5-phosphatase activity, is defined by the Gene Ontology as catalysis of the reactions: D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate, and 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate. In other words, it is the enzymatic removal of the phosphate group at the 5-position of inositol polyphosphate substrates, producing a phosphate ion and a lower-phosphorylated inositol product. This activity is distinct from 3-phosphatases and 4-phosphatases because it specifically targets the 5-position, and it can act on both soluble inositol polyphosphates and, for some enzymes, on lipid phosphoinositides.
Why Is inositol-polyphosphate 5-phosphatase activity Important in Cell Biology?
GO:0004445 is important because it controls the lifetime of inositol polyphosphate second messengers that regulate calcium release, Akt activation, cytoskeletal dynamics, and gene expression. By removing the 5-phosphate, these enzymes set the threshold for PI3K-dependent signaling and prevent excessive or prolonged activation of downstream effectors. Consequently, altered 5-phosphatase activity is linked to cancer, immune disorders, metabolic disease, and impaired neural regeneration, making the term a focal point for both mechanistic and therapeutic research.
• Terminates Ins(1,4,5)P3 signaling, thereby limiting calcium release from intracellular stores.
• Converts Ins(1,3,4,5)P4 to Ins(1,3,4)P3, shaping the inositol tetrakisphosphate signaling pool.
• Regulates PI3K-dependent Akt activation through lipid 5-phosphatase activity of SHIP1 and SHIP2.
• Controls actin remodeling and membrane ruffling via PIPP and related 5-phosphatases.
• Promotes corticospinal tract axon sprouting after CNS trauma through INPP5K.
• Modulates immune cell activation and cytokine signaling via SHIP1.
• Contributes to metabolic regulation and insulin sensitivity through SHIP2.
• Provides a biochemical node for plant and parasite 5-phosphatases such as Gs5PTase8.
• Serves as a target for domain-specific mutational analysis because C2 and SH2 domains regulate catalysis.
• Enables experimental separation of soluble inositol phosphate versus lipid phosphoinositide hydrolysis.
Molecular Mechanism of inositol-polyphosphate 5-phosphatase activity
Substrate recognition and binding
In simple terms: The enzyme first grabs the inositol phosphate substrate in the right orientation.
Inositol polyphosphate 5-phosphatases recognize the inositol ring and its phosphate groups through a conserved catalytic domain that positions the 5-phosphate for hydrolysis. For SHIP1 and SHIP2, the C2 domain contributes to substrate binding and regulates access to the catalytic site, as shown by structural and functional studies. The enzyme can act on soluble substrates such as Ins(1,4,5)P3 and Ins(1,3,4,5)P4, and some family members also accept lipid substrates such as phosphatidylinositol 3,4,5-trisphosphate.
Catalytic hydrolysis of the 5-phosphate
In simple terms: The enzyme cuts off the phosphate at the 5-position using water.
The catalytic reaction removes the 5-phosphate from D-myo-inositol 1,4,5-trisphosphate to yield myo-inositol 1,4-bisphosphate and phosphate, and from 1D-myo-inositol 1,3,4,5-tetrakisphosphate to yield 1D-myo-inositol 1,3,4-trisphosphate and phosphate. This hydrolysis is metal-dependent in many 5-phosphatases, and the reaction is terminated when the substrate leaves the active site or when the enzyme is inhibited. The reaction is a phosphomonoesterase step, consistent with the synonym inositol phosphate 5-phosphomonoesterase activity.
Domain architecture and regulation
In simple terms: Extra domains on the enzyme act like switches that turn activity up or down.
SHIP1 and SHIP2 contain SH2, proline-rich, and C2 domains in addition to the catalytic 5-phosphatase domain, and the C2 domain specifically regulates inositol 5-phosphatase activity. The signaling inositol polyphosphate-5-phosphatase characterized by Jefferson et al. is regulated by GRB2 association, demonstrating that protein-protein interactions can modulate catalysis. PIPP localizes to membrane ruffles and regulates phosphoinositide 3-kinase-dependent neurite elongation, showing that subcellular targeting is part of the regulatory logic.
Downstream signaling consequences
In simple terms: Removing the 5-phosphate changes what the cell does next.
By converting Ins(1,4,5)P3 to Ins(1,4)P2, the enzyme reduces calcium mobilization and terminates a key second-messenger signal. Lipid 5-phosphatase activity of SHIP1 and SHIP2 converts phosphatidylinositol 3,4,5-trisphosphate to phosphatidylinositol 3,4-bisphosphate, thereby dampening Akt activation and PI3K-dependent growth signals. INPP5K enhances sprouting of corticospinal tract axons after CNS trauma, linking the activity to neural repair programs.
Assays and measurement
In simple terms: Scientists measure this activity by watching how fast the phosphate is released.
Biochemical assays use radiolabeled or fluorescent inositol phosphate substrates to quantify phosphate release, as described for signaling inositol polyphosphate-5-phosphatase and for SHIP1/SHIP2 domain studies. Recombinant expression and purification of 5-phosphatases such as Gs5PTase8 enable direct activity measurements and kinetic characterization. Cellular readouts include phosphoinositide profiling, Akt phosphorylation, and cytoskeletal or axon outgrowth phenotypes.
Key Genes Involved in GO:0004445 inositol-polyphosphate 5-phosphatase activity
The following genes and proteins carry or regulate inositol-polyphosphate 5-phosphatase activity and are commonly used in mechanistic studies.
| Gene | Major Role | Research Relevance |
|---|---|---|
| INPP5D (SHIP1) | Hematopoietic 5-phosphatase acting on Ins(1,4,5)P3 and PI(3,4,5)P3 | Immune signaling, C2-domain regulation, cancer models |
| INPPL1 (SHIP2) | Ubiquitous 5-phosphatase regulating PI3K/Akt and insulin signaling | Metabolic disease, C2-domain structure-function |
| INPP5K | Inositol polyphosphate 5-phosphatase in neural cells | Axon sprouting after CNS trauma |
| INPP5J (PIPP) | 5-phosphatase localized to membrane ruffles | Neurite elongation, actin remodeling |
| INPP5B | Type II inositol 1,4,5-trisphosphate 5-phosphatase | Comparative enzymology of 5-phosphatases |
| OCRL | 5-phosphatase mutated in Lowe syndrome | Phosphoinositide signaling and disease models |
| SYNJ1 | Synaptojanin 1, a polyphosphoinositide 5-phosphatase | Synaptic vesicle recycling and neurodegeneration |
| SYNJ2 | Synaptojanin 2, 5-phosphatase | Membrane trafficking and signaling |
| INPP5A | Type I inositol-polyphosphate 5-phosphatase | Soluble inositol phosphate hydrolysis |
| INPP5E | Ciliary 5-phosphatase | Ciliopathies and phosphoinositide signaling |
| Gs5PTase8 | Wild soybean 5-phosphatase | Prokaryotic expression and activity assays |
| GRB2 | Adapter protein associating with signaling 5-phosphatase | Regulation of 5-phosphatase activity |
| PIK3CA | PI3K catalytic subunit generating PI(3,4,5)P3 | Upstream input to 5-phosphatase pathways |
| AKT1 | Downstream kinase inhibited by SHIP1/SHIP2 activity | Readout of 5-phosphatase function |
| ACTB | Actin cytoskeleton component | Membrane ruffle and neurite phenotypes |
| CDC42 | Rho GTPase regulating actin | Cytoskeletal readouts of 5-phosphatase loss |
| ITPR1 | Ins(1,4,5)P3 receptor | Calcium signaling downstream of 5-phosphatase activity |
| PTPN11 | Tyrosine phosphatase in RTK signaling | Cross-talk with phosphoinositide pathways |
How Is inositol-polyphosphate 5-phosphatase activity Regulated?
Inositol-polyphosphate 5-phosphatase activity is regulated at multiple levels. The C2 domain of SHIP1 and SHIP2 directly modulates inositol 5-phosphatase activity, and domain-deletion studies show that removing or mutating the C2 domain changes catalytic output. Protein-protein interactions also regulate activity; the signaling inositol polyphosphate-5-phosphatase is affected by GRB2 association. Subcellular localization controls access to substrates, as PIPP localizes to membrane ruffles where phosphoinositides are enriched. Upstream PI3K signaling generates lipid substrates for SHIP1 and SHIP2, creating a feedback loop in which 5-phosphatase activity tunes the strength and duration of PI3K-dependent signals. In neural contexts, INPP5K activity is linked to axon sprouting programs after trauma, indicating that extracellular cues and injury signals can influence the functional outcome of the activity.
inositol-polyphosphate 5-phosphatase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| INPP5D (SHIP1) | Immune signaling and hematologic malignancy | Knockout and C2-domain point-mutation cell lines |
| INPPL1 (SHIP2) | Metabolic disease and insulin resistance | Knock-in of catalytic-dead or C2-mutant alleles |
| INPP5K | CNS trauma and axon regeneration | Knockout neurons and axon outgrowth assays |
| INPP5J (PIPP) | Neurite elongation and actin remodeling | Overexpression and knockdown in neuronal cells |
| OCRL | Lowe syndrome and phosphoinositide trafficking | Patient-derived cells and knock-in models |
Cancer and PI3K pathway dysregulation
SHIP1 and SHIP2 are 5-phosphatases that counteract PI3K signaling by converting PI(3,4,5)P3 to PI(3,4)P2, and their C2 domains regulate this activity. Loss or reduced 5-phosphatase activity can therefore amplify Akt activation and promote growth signals relevant to cancer. Because the catalytic and regulatory domains are separable, domain-specific mutations are needed to determine whether disease-associated variants affect catalysis directly or alter protein interactions.
Neurological injury and axon regeneration
INPP5K enhances sprouting of corticospinal tract axons after central nervous system trauma, indicating that 5-phosphatase activity supports neural repair programs. PIPP regulates phosphoinositide 3-kinase-dependent neurite elongation, further linking 5-phosphatase function to neuronal morphogenesis. These findings suggest that modulating 5-phosphatase activity could influence recovery after injury, although the precise substrates and downstream effectors remain an active area of study.
Immune and metabolic disorders
SHIP1 is a major 5-phosphatase in hematopoietic cells, and its activity shapes immune receptor signaling through phosphoinositide hydrolysis. SHIP2 regulates insulin sensitivity and metabolic signaling, and its C2 domain contributes to catalytic control. Dysregulated 5-phosphatase activity in these contexts has been associated with immune dysfunction and metabolic disease, making these enzymes candidates for targeted experimental models.
Inherited phosphoinositide signaling disorders
Several 5-phosphatases, including OCRL, INPP5E, and synaptojanins, are linked to inherited disorders of phosphoinositide metabolism and membrane trafficking. Although GO:0004445 describes the catalytic activity shared by these enzymes, the disease phenotypes depend on the specific protein context, localization, and substrate repertoire. Comparative studies of 5-phosphatase family members help distinguish shared catalytic mechanisms from isoform-specific disease mechanisms.
From inositol-polyphosphate 5-phosphatase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of 5-phosphatase activity alter PI3K/Akt signaling? | CRISPR knockout of SHIP1 or SHIP2 in cell lines |
| Does the C2 domain regulate catalytic activity? | Point mutations or domain deletions in SHIP1/SHIP2 |
| Does a disease variant affect catalysis or localization? | Knock-in of the variant allele with tagged enzyme |
| Does increased 5-phosphatase activity change axon growth? | Overexpression of INPP5K in neurons |
| Does 5-phosphatase activity control membrane ruffling? | Overexpression or knockout of PIPP in motile cells |
| Can plant 5-phosphatase activity be measured in vitro? | Recombinant expression of Gs5PTase8 |
How to Study the inositol-polyphosphate 5-phosphatase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Radioactive inositol phosphate assay | Phosphate release from labeled substrates | Quantifying 5-phosphatase activity in lysates or recombinant enzyme |
| Fluorescent substrate assay | Real-time hydrolysis of inositol phosphates | Kinetic characterization of 5-phosphatases |
| Phosphoinositide profiling | Levels of PI(3,4,5)P3 and related lipids | Assessing SHIP1/SHIP2 lipid 5-phosphatase activity |
| Akt phosphorylation immunoblot | PI3K pathway activation | Readout of 5-phosphatase loss or gain |
| Calcium imaging | Ins(1,4,5)P3-dependent calcium release | Functional consequence of 5-phosphatase activity |
| Live-cell microscopy | Membrane ruffling and neurite elongation | Spatial phenotypes of PIPP and INPP5K |
| Recombinant protein purification | Enzyme amount and purity | In vitro activity assays for Gs5PTase8 and other 5-phosphatases |
| Domain-deletion mutagenesis | Contribution of C2, SH2, or proline-rich domains | Mapping regulatory domains in SHIP1/SHIP2 |
Biochemical activity assays
Direct measurement of GO:0004445 uses inositol polyphosphate substrates and detects phosphate release or product formation. Signaling inositol polyphosphate-5-phosphatase activity has been characterized with such assays, and SHIP1/SHIP2 domain studies use similar approaches to quantify catalysis. Recombinant purification of 5-phosphatases such as Gs5PTase8 enables kinetic analysis and substrate specificity testing.
Phosphoinositide and inositol phosphate profiling
Lipid and soluble inositol phosphate profiling can reveal changes in substrate and product pools after genetic perturbation. Because 5-phosphatases act on both Ins(1,4,5)P3 and PI(3,4,5)P3, profiling helps distinguish soluble versus lipid substrate contributions. These measurements are often paired with activity assays to confirm that observed changes are due to 5-phosphatase activity rather than upstream synthesis.
Signaling readouts and imaging
Downstream readouts such as Akt phosphorylation, calcium mobilization, and cytoskeletal dynamics report the functional consequences of 5-phosphatase activity. Imaging of membrane ruffles and neurite elongation provides spatial information about where the activity matters, as shown for PIPP and INPP5K. Combining imaging with genetic perturbation helps link the catalytic activity to specific cellular phenotypes.
Genetic perturbation and rescue
Knockout, point-mutation, and rescue experiments are used to test whether a specific gene product is responsible for a measured 5-phosphatase activity. Catalytic-dead mutants can separate enzymatic activity from scaffolding functions, while wild-type rescue confirms specificity. These approaches are essential when multiple 5-phosphatases are expressed in the same cell type.
How CRISPR Can Be Used to Study GO:0004445 inositol-polyphosphate 5-phosphatase activity
Knockout
CRISPR knockout of 5-phosphatase genes such as INPP5D, INPPL1, or INPP5K removes the enzyme and reveals its contribution to phosphoinositide signaling and cellular phenotypes. Knockout cells can be used to measure changes in Ins(1,4,5)P3 turnover, Akt activation, and cytoskeletal dynamics. Because multiple 5-phosphatases may compensate, knockout studies often require validation with activity assays and rescue experiments.
Point Mutation
Point mutations in the catalytic domain or in regulatory domains such as the C2 domain can separate enzymatic activity from protein-protein interaction functions. For example, mutations that impair SHIP1 or SHIP2 catalysis can be compared with mutations that alter C2-domain regulation to determine which function drives a phenotype. Point-mutation models are also useful for testing disease-associated variants identified in sequencing studies.
Knock-in
Knock-in of tagged or mutant 5-phosphatase alleles allows endogenous expression levels and localization to be preserved while tracking the protein. Tagged knock-in models can be used to measure activity in specific subcellular compartments and to correlate localization with substrate access. Knock-in of patient variants provides a physiologically relevant context for studying altered 5-phosphatase function.
Overexpression
Overexpression of wild-type or mutant 5-phosphatases can amplify the activity and reveal gain-of-function phenotypes such as reduced Akt signaling or enhanced neurite outgrowth. Overexpression of PIPP has been used to study phosphoinositide 3-kinase-dependent neurite elongation, and INPP5K overexpression enhances axon sprouting. Overexpression systems are also useful for producing recombinant enzyme for biochemical assays.
How EDITGENE Supports inositol-polyphosphate 5-phosphatase activity Research
Researchers studying inositol-polyphosphate 5-phosphatase activity-related genes often need to determine whether a candidate gene is causally involved in a signaling or disease phenotype. EDITGENE provides CRISPR-based cell model services that enable precise knockout, point mutation, knock-in, and overexpression of 5-phosphatase genes, along with library screening and bioinformatics support to interpret the resulting data.
Contact EDITGENE today to design your custom CRISPR model for inositol-polyphosphate 5-phosphatase activity research.
Frequently Asked Questions About inositol-polyphosphate 5-phosphatase activity
What is inositol-polyphosphate 5-phosphatase activity?
It is the enzymatic activity defined by GO:0004445 that removes the 5-phosphate from inositol polyphosphates such as Ins(1,4,5)P3 and Ins(1,3,4,5)P4, producing lower-phosphorylated products and phosphate.
What reaction does GO:0004445 catalyze?
It catalyzes D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate, and 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
What genes are involved in inositol-polyphosphate 5-phosphatase activity?
Key genes include INPP5D (SHIP1), INPPL1 (SHIP2), INPP5K, INPP5J (PIPP), INPP5B, OCRL, SYNJ1, SYNJ2, INPP5A, and INPP5E, among others.
How is inositol-polyphosphate 5-phosphatase activity regulated?
It is regulated by domains such as the C2 domain of SHIP1 and SHIP2, by protein-protein interactions such as GRB2 association, and by subcellular localization that controls substrate access.
What diseases are linked to inositol-polyphosphate 5-phosphatase activity?
Altered activity has been linked to cancer, immune and metabolic disorders, neurological injury, and inherited phosphoinositide signaling disorders involving OCRL, INPP5E, and synaptojanins.
How do you measure inositol-polyphosphate 5-phosphatase activity?
Common methods include radioactive or fluorescent inositol phosphate assays, phosphoinositide profiling, Akt phosphorylation immunoblots, calcium imaging, and live-cell microscopy.
What is the difference between SHIP1 and SHIP2 5-phosphatase activity?
Both SHIP1 and SHIP2 hydrolyze phosphoinositides, but their C2 domains differ in how they regulate catalytic activity and substrate access, which affects their roles in immune versus metabolic signaling.
Can CRISPR be used to study inositol-polyphosphate 5-phosphatase activity?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression models are used to test the causal role of specific 5-phosphatase genes in signaling and disease phenotypes.
What substrates are used to assay GO:0004445?
Assays typically use D-myo-inositol 1,4,5-trisphosphate and 1D-myo-inositol 1,3,4,5-tetrakisphosphate, and some enzymes also act on phosphatidylinositol 3,4,5-trisphosphate.
Why is inositol-polyphosphate 5-phosphatase activity important for neurons?
INPP5K enhances corticospinal tract axon sprouting after CNS trauma, and PIPP regulates phosphoinositide 3-kinase-dependent neurite elongation, linking the activity to neural repair and morphogenesis.
Conclusion
GO:0004445, inositol-polyphosphate 5-phosphatase activity, is a central enzymatic function that terminates and reshapes inositol polyphosphate and phosphoinositide signals. Its catalytic removal of the 5-phosphate controls calcium signaling, PI3K/Akt activation, cytoskeletal dynamics, and neural repair, with SHIP1, SHIP2, INPP5K, and PIPP serving as key experimental models. Because the activity is embedded in multidomain proteins, precise genetic models are needed to separate catalysis from regulation. CRISPR knockout, point-mutation, knock-in, and overexpression approaches, combined with biochemical and imaging readouts, provide a robust framework for dissecting how 5-phosphatases contribute to health and disease.
References
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- 3. Jefferson AB et al.. 1997. Signaling inositol polyphosphate-5-phosphatase. Characterization of activity and effect of GRB2 association.. J Biol Chem 272(9):5983-8 PMID: 9038219
- 4. Mochizuki Y et al.. 1999. Novel inositol polyphosphate 5-phosphatase localizes at membrane ruffles.. J Biol Chem 274(51):36790-5 PMID: 10593988
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