IndraLab

Statements

AKT binds USP33. 5 / 5
| 1 4
reach
"We observed that whereas the interaction between Akt and USP33 increased under the desensitization conditions (Fig. 6A), this response was absent when we used USP33 harboring a mutated T154 residue, which is a known consensus Akt phosphorylation site (Fig. 6B)."
36658650
sparser
"The desensitization-induced increase in the interaction between Akt and USP33 (Fig.  xref A), and the nuclear translocation of Gβγ and arrestin (Fig.  xref B) were also inhibited by pretreatment with AG1478."
39468452
sparser
"Indeed, biochemical changes in cellular components constituting the GPCR desensitization cascade were evoked when cells were treated with EGF, such as phosphorylation of Src (Fig.  xref A), Akt (Fig.  xref B), the interaction between Akt and USP33 (Fig.  xref C), which culminated in the deubiquitination of arrestins (Fig.  xref D)."
39468452
sparser
"Given that USP33 and USP14 have high sequence homology, and that the 149 KARGLT 154 sequence of USP33 possesses a consensus Akt phosphorylation site (RxRxxS/T) [ xref ], it is assumed that Akt would similarly interact with USP33."
36658650
sparser
"We observed that whereas the interaction between Akt and USP33 increased under the desensitization conditions (Fig.  xref A), this response was absent when we used USP33 harboring a mutated T154 residue, which is a known consensus Akt phosphorylation site (Fig.  xref B)."
36658650