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Literature summary for 3.1.3.66 extracted from

  • Ivetac, I.; Gurung, R.; Hakim, S.; Horan, K.A.; Sheffield, D.A.; Binge, L.C.; Majerus, P.W.; Tiganis, T.; Mitchell, C.A.
    Regulation of PI(3)K/Akt signalling and cellular transformation by inositol polyphosphate 4-phosphatase-1 (2009), EMBO Rep., 10, 487-493.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
full-length 4-ptase-1 cDNA subcloned into the EcoRI site of pWzl-Hygromycin vector Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
embryonic fibroblast cell line
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 Mus musculus
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Synonyms

Synonyms Comment Organism
4-ptase-1
-
 Mus musculus
inositol polyphosphate 4-phosphatase-1
-
 Mus musculus

Expression

Organism Comment Expression
Mus musculus level of 4-ptase-1 protein expressed in reconstituted embryonic fibroblasts reveals a 5fold increase relative to endogenous 4-ptase-1 in +/+MEFs up

General Information

General Information Comment Organism
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 Mus musculus
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 Mus musculus