Table 2.
Separation of enzymatic function variants
| Variant | Lipid phosphatase activity in vitro | PKB suppression in vivo | Protein phosphatase activity | Cell growth inhibition | Migration suppression | DNA repaira | References |
|---|---|---|---|---|---|---|---|
| Wild-type | + | + | + | + | + | + | Myers et al. 1998; Gildea et al. 2004; Davidson et al. 2010; Bassi et al. 2013; Vuono et al. 2016 |
| Y138Lb | + | + | − | + | +/− | − | Davidson et al. 2010; Tibarewal et al. 2012; Vuono et al. 2016 |
| G129Eb | − | − | + | − | +/− | + | Myers et al. 1998; Gildea et al. 2004; Davidson et al. 2010; Bassi et al. 2013; Vuono et al. 2016 |
| C124Sb | − | − | − | − | +/− | − | Myers et al. 1998; Gildea et al. 2004; Davidson et al. 2010; Bassi et al. 2013; Vuono et al. 2016 |
| Y138C | + | + | − | + | NS | NS | Tibarewal et al. 2012 |
| M134L | − | − | + | − | NS | NS | Myers et al. 1998; Han et al. 2000 |
Included are thermodynamically stable PTEN mutants for which both lipid and protein phosphatase activities have been measured. Wild-type, Y138L, G129E, and C124S are commonly used in PTEN studies.
NS, not studied.
aDNA repair capabilities as reported by Bassi et al. (2013) and Vuono et al. (2016).
bSentinel variant.