Brassica rapa DSP/PTEN
※ PTEN family introduction PTEN (phosphatase and tensin homolog deleted on chromosome ten) phosphatase is a conserved family of DUSP phosphatase, which could dephosphorylate tyrosine-, serine- and threonine-phosphorylated proteins. PTEN also acts as lipid phosphatase, which dephosphorylates D3-phosphorylated inositol phospholopids (1). PTEN negatively regulates PI3 kinase-Akt signaling pathway by converting second messenger phosphatidylinositol 3,4,5-triphosphate (PIP3) into phosphatidylinositol 4,5-bisphosphate (PIP2). This pathway plays an important role in controlling cell proliferation, growth and survival (2). In addition to its dominant inhibitory activity in the PI3 kinase-Akt pathway, PTEN also possess potential protein phosphatase activity for its sequence similarity with PTP domain and this remains more understood. Reference
1. Patterson, K.I., Brummer, T., O'Brien, P.M. and Daly, R.J. (2009) Dual-specificity phosphatases: critical regulators with diverse cellular targets. Biochem J, 418, 475-489. PMID: 19228121
2. Wang, X. and Jiang, X. (2008) PTEN: a default gate-keeping tumor suppressor with a versatile tail. Cell Res, 18, 807-816. PMID: 18626510
There are 16 genes. Reviewed (0)
or Unreviewed (16) 
※ PTEN family introduction PTEN (phosphatase and tensin homolog deleted on chromosome ten) phosphatase is a conserved family of DUSP phosphatase, which could dephosphorylate tyrosine-, serine- and threonine-phosphorylated proteins. PTEN also acts as lipid phosphatase, which dephosphorylates D3-phosphorylated inositol phospholopids (1). PTEN negatively regulates PI3 kinase-Akt signaling pathway by converting second messenger phosphatidylinositol 3,4,5-triphosphate (PIP3) into phosphatidylinositol 4,5-bisphosphate (PIP2). This pathway plays an important role in controlling cell proliferation, growth and survival (2). In addition to its dominant inhibitory activity in the PI3 kinase-Akt pathway, PTEN also possess potential protein phosphatase activity for its sequence similarity with PTP domain and this remains more understood. Reference
1. Patterson, K.I., Brummer, T., O'Brien, P.M. and Daly, R.J. (2009) Dual-specificity phosphatases: critical regulators with diverse cellular targets. Biochem J, 418, 475-489. PMID: 19228121
2. Wang, X. and Jiang, X. (2008) PTEN: a default gate-keeping tumor suppressor with a versatile tail. Cell Res, 18, 807-816. PMID: 18626510
There are 16 genes. Reviewed (0)
or Unreviewed (16)