Inositol Polyphosphate 5‐Phosphatases: Lipid Phosphatases With Flair [PDF]
AbstractRecent studies have identified the inositol polyphosphate 5‐phosphatases as a large family of signal modifying enzymes comprising 10 mammalian and 4 yeast family members. A number of investigations including gene‐targeted deletion of 5‐phosphatases in mice have demonstrated that these enzymes regulate many important cellular events including ...
Christina A, Mitchell +5 more
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Mutations in INPP5E, encoding inositol polyphosphate-5-phosphatase E, link phosphatidyl inositol signaling to the ciliopathies [PDF]
Phosphotidylinositol (PtdIns) signaling is tightly regulated both spatially and temporally by subcellularly localized PtdIns kinases and phosphatases that dynamically alter downstream signaling events. Joubert syndrome is characterized by a specific midbrain-hindbrain malformation ('molar tooth sign'), variably associated retinal dystrophy ...
Bielas SL +24 more
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Inositol polyphosphate 5‐phosphatases; new players in the regulation of cilia and ciliopathies
Phosphoinositides regulate numerous cellular events via the recruitment and activation of multiple lipid‐binding effector proteins. The precise temporal and spatial regulation of phosphoinositide signals by the co‐ordinated activities of phosphoinositide kinases and phosphatases is essential for homeostasis and development.
Conduit, Sarah E. +2 more
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The Inositol Polyphosphate 5-Phosphatase PIPP Regulates AKT1-Dependent Breast Cancer Growth and Metastasis [PDF]
Metastasis is the major cause of breast cancer mortality. Phosphoinositide 3-kinase (PI3K) generated PtdIns(3,4,5)P3 activates AKT, which promotes breast cancer cell proliferation and regulates migration. To date, none of the inositol polyphosphate 5-phosphatases that inhibit PI3K/AKT signaling have been reported as tumor suppressors in breast cancer ...
Ooms, LM +16 more
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Expansion and Functional Divergence of Inositol Polyphosphate 5-Phosphatases in Angiosperms. [PDF]
Inositol polyphosphate 5-phosphatase (5PTase), a key enzyme that hydrolyzes the 5′ position of the inositol ring, has essential functions in growth, development, and stress responses in plants, yeasts, and animals. However, the evolutionary history and patterns of 5PTases have not been examined systematically.
Zhang Z +8 more
europepmc +4 more sources
Properties of Type II Inositol Polyphosphate 5-Phosphatase [PDF]
We have isolated additional cDNA clones encoding type II inositol polyphosphate 5-phosphatase (5-phosphatase II) resulting in a combined cDNA of 3076 nucleotides encoding a protein of 942 amino acids. The 5-phosphatase II hydrolyzed both Ins(1,4,5)P3 to Ins(1,4)P2 and the phospholipid PtdIns(4,5)P2 to PtdIns(4)P both in vitro and in vivo. There are two
A B, Jefferson, P W, Majerus
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Novel inositol polyphosphate 5-phosphatase localizes at membrane ruffles. [PDF]
We have cloned a novel inositol polyphosphate 5-phosphatase from the rat brain cDNA library. It contains two highly conserved 5-phosphatase motifs, both of which are essential for its enzymatic activity. Interestingly, the proline content of this protein is high and concentrated in its N- and C-terminal regions.
Y, Mochizuki, T, Takenawa
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Crystal Structures of Type-II Inositol Polyphosphate 5-Phosphatase INPP5B with Synthetic Inositol Polyphosphate Surrogates Reveal New Mechanistic Insights for the Inositol 5-Phosphatase Family [PDF]
The inositol polyphosphate 5-phosphatase INPP5B hydrolyzes the 5-phosphate group from water- and lipid-soluble signaling messengers. Two synthetic benzene and biphenyl polyphosphates (BzP/BiPhPs), simplified surrogates of inositol phosphates and phospholipid headgroups, were identified by thermodynamic studies as potent INPP5B ligands.
Mills SJ +5 more
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Phosphorylation of Platelet Pleckstrin Activates Inositol Polyphosphate 5-Phosphatase I [PDF]
Pleckstrin is the major substrate phosphorylated on serine and threonine in response to stimulation of human platelets by thrombin (Abrams, C. S., Zhao, W., Belmonte, E., and Brass, L. F. (1995) J. Biol. Chem. 270, 23317-23321). We now show that pleckstrin in platelets is in a complex with inositol polyphosphate 5-phosphatase I (5-phosphatase I).
V, Auethavekiat +2 more
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Identification and Characterization of a Novel Inositol Polyphosphate 5-Phosphatase [PDF]
We have identified a cDNA encoding a novel inositol polyphosphate 5-phosphatase. It contains two highly conserved catalytic motifs for 5-phosphatase, has a molecular mass of 51 kDa, and is ubiquitously expressed and especially abundant in skeletal muscle, heart, and kidney.
T, Ijuin +5 more
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