| HRA010555
(Open Access)
|
Ubiquitin modifications play diverse and predominant roles in virous physiological and pathological processes. However, the impact of atypical ubiquitin modification on AKT and its potential role in tumorigenesis remain largely unclear. Although K48-linked ubiquitin-mediated degradation of phosphorylated AKT and K63-linked ubiquitin-mediated activation of AKT have been reported, whether and how AKT undergoes non-canonical types of ubiquitination in pathophysiological conditions have not been defined.Through systematic ubiquitin analyses, we have observed that AKT undergoes K27-linked ubiquitination to imply its negative regulation conditions |
