Reactome | PI(3,4)P2 is dephosphorylated to PI4P by PTEN at the plasma membrane

PI(3,4)P2 is dephosphorylated to PI4P by PTEN at the plasma membrane

Stable Identifier

R-HSA-1676149

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane, cytosol

ReviewStatus

5/5

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PI(3,4)P2 is dephosphorylated to PI4P by PTEN at the plasma membrane

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At the plasma membrane, phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase aka phosphatase and tensin homolog (PTEN) dephosphorylates phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) to phosphatidylinositol 4-phosphate (PI4P) (Myers et al. 1998, Das et al. 2003).
Early studies indicated that magnesium ion, Mg2+, was needed for the catalytic activity of PTEN isolated from bovine thymus (Kabuyama et al. 1996). Subsequent studies have shown that PTEN was catalytically active in buffers free of magnesium and magnesium was not detected as part of the PTEN crystal (Lee et al. 1999).

Literature References

PubMed ID	Title	Journal	Year
8681945	Purification and characterization of the phosphatidylinositol-3,4,5-trisphosphate phosphatase in bovine thymus Fukui, Y, Kabuyama, Y, Homma, Y, Nakatsu, N	Eur. J. Biochem.	1996
9811831	The lipid phosphatase activity of PTEN is critical for its tumor supressor function Stolarov, JP, van der Kaay, J, Myers, MP, Pass, I, Downes, CP, Batty, IH, Wigler, MH, Tonks, NK, Hemmings, BA	Proc Natl Acad Sci U S A	1998
12808147	Membrane-binding and activation mechanism of PTEN Das, S, Cho, W, Dixon, JE	Proc Natl Acad Sci U S A	2003
10555148	Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association Georgescu, MM, Pavletich, NP, Shi, Y, Maehama, T, Pandolfi, P, Yang, H, Lee, JO, Dixon, JE, Di Cristofano, A	Cell	1999