EC Number   |
General Information |
Reference |
|---|
   3.1.3.66 | malfunction |
ananlysis of the role of 4-phosphatase I in the regulation of PtdIns(3,4)P2 in platelets in the weeble mouse model, the mice are viable, but lack platelet 4-phosphatase I, overview. Weeble chimeric mice have a propensity for thrombosis using a carotid artery injury model |
713689 |
| 3.1.3.66 | malfunction |
in mouse embryonic fibroblasts lacking 4-ptase-1 (-/-MEFs), the Akt-pleckstrin homology domain is constitutively membrane-associated both in serum-starved and agonist-stimulated cells. 4-Ptase-1-deficient cells show increased Akt signalling. Loss of 4-ptase-1 results in increased cell proliferation and decreased apoptosis. Loss of function of 4-ptase-1 leads to increased and sustained growth factor-stimulated levels of pSer473/Thr308-Akt and Akt phospho-substrates |
708332 |
| 3.1.3.66 | malfunction |
inositol polyphosphate 4-phosphatase-II knockdown in estrogen receptor-positive breast cancer cells increased Akt activation, cell proliferation, and xenograft tumor growth |
716766 |
| 3.1.3.66 | malfunction |
Inpp4a weeble mutant has a frame shift mutation in Inpp4a and is characterized by an early onset recessive cerebellar ataxia. In the Inpp4a weeble mutant, Purkinje cells are lost in a specific temporal and spatial pattern: Purkinje cells are lost at early perinatal timepoints. Prior to the appearance of climbing fibers in the developing molecular layer, the Inpp4a weeble mutant has a normal complement of Purkinje cells and they are properly positioned, degeneration and reactive gliosis are present at postnatal day 5 and progress rapidly in a defined pattern of patches. Purkinje cell loss in the Inpp4awbl mutant is due to glutamate excitotoxicity initiated by the climbing fiber, whereby Eaat4 may exert a protective effect |
710384 |
| 3.1.3.66 | malfunction |
knocking down the expression of INPP4B in human epithelial cells, like knockdown of PTEN, results in enhanced Akt activation and anchorage-independent growth and enhanced overall motility. INPP4B knockdown results in increased migratory and invasive behavior of mammary epithelial cells. Dual knockdown of INPP4B and PTEN results in cellular senescence and causes a more prolonged phosphorylation of AKT at Thr308 than that caused by knocking down either protein alone. INPP4B knockdown in MCF-10A mammary epithelial cells results in distorted acini architecture in three-dimensional culture |
707954 |
| 3.1.3.66 | malfunction |
lung-specific knockdown of INPP4A by siRNA induces spontaneous inflammation in mice possibly by activating the PI3K-Akt pathway. In mice with experimental asthma, further knockdown of INPP4A by siRNA leads to a severe asthma phenotype, whereas overexpression of INPP4A reverses airway hyper-responsiveness (AHR) and airway inflammation in allergic mice |
732559 |
| 3.1.3.66 | malfunction |
silenced INPP4B expression in malignant proerythroblast is associated with increased activated-Akt levels that can be alleviated by the reexpression of INPP4B. Knockdown of INPP4B in LNCaP cells enhances proliferation |
714648 |
| 3.1.3.66 | malfunction |
the insertion of Tgkd 3 of the Inpp4b gene is associated with decreased expression of Inpp4b and changes in intracellular PI3 Kinase/AKT signaling in follicular granulosa cells. This is associated with several follicular defects including oocytes trapped within luteinized follicles |
731696 |
| 3.1.3.66 | more |
INPP4B is regulated by androgens at the level of transcription. INPP4B mRNA expression is induced in both LNCaP and VCaP AR-expressing prostate cancer cells. INPP4B and PTEN expression are correlated with the recurrence rate of patients with high and low expression levels of the proliferation marker Ki67 |
714648 |
| 3.1.3.66 | physiological function |
4-ptase-1 controls the activation of Akt and thereby cell proliferation, survival and tumorigenesis. In mouse embryonic fibroblasts (+/+MEFs), the Akt-pleckstrin homology domain is detected at the plasma membrane following serum stimulation |
708332 |
