| First Author | Nawa M | Year | 2013 |
| Journal | BMC Biochem | Volume | 14 |
| Pages | 27 | PubMed ID | 24156551 |
| Mgi Jnum | J:213891 | Mgi Id | MGI:5586787 |
| Doi | 10.1186/1471-2091-14-27 | Citation | Nawa M, et al. (2013) KCTD20, a relative of BTBD10, is a positive regulator of Akt. BMC Biochem 14:27 |
| abstractText | BACKGROUND: BTBD10 binds to Akt and protein phosphatase 2A (PP2A) and inhibits the PP2A-mediated dephosphorylation of Akt, thereby keeping Akt activated. Previous studies have suggested that BTBD10 plays an important role in preventing motor neuronal death and accelerating the growth of pancreatic beta cells. Because levels of BTBD10 expression are much lower in many non-nervous tissues than nervous tissues, there may be a relative of BTBD10 that has BTBD10-like function in non-neuronal cells. RESULTS: A 419-amino-acid BTBD10-like protein, named KCTD20 (potassium channel tetramerization protein domain containing 20), was to found to bind to all Akt isoforms and PP2A. Overexpression of KCTD20 increased Akt phosphorylation at Thr308, as BTBD10 did, which suggests that KCTD20 as well as BTBD10 positively regulates the function of Akt. KCTD20 was ubiquitously expressed in non-nervous as well as nervous tissues. CONCLUSIONS: KCTD20 is a positive regulator of Akt and may play an important role in regulating the death and growth of some non-nervous and nervous cells. |
