More recently, an interaction between USP7 and the EBNA1 protein of Epstein-Barr virus (EBV) (another herpesvirus ) was also discovered.  This interaction is particularly interesting given the oncogenic potential (potential to cause cancer) of EBV, which is associated with several human cancers. EBNA1 can compete with p53 for binding USP7. Stabilization by USP7 is important for the tumor suppressor function of p53. In cells, EBNA1 can sequester USP7 from p53 and thus attenuate stabilization of p53, rendering the cells predisposed to turning cancerous. Compromising the function of p53 by sequestering USP7 is one way EBNA1 can contribute to the oncogenic potential of EBV. Additionally, human USP7 was also shown to form a complex with GMPS and this complex is recruited to EBV genome sequences.  USP7 was shown to be important for histone H2B deubiquitination in human cells and for deubiquitination of histone H2B incorporated in the EBV genome. Thus USP7 may also be important for regulation of viral gene expression.
As for mechanisms of action, ecydsteroids seem to be able to cause a rapid Ca2+ influx in myocytes which leads to phosphorylation of Akt and thus protein synthesis.  This effect occurs after 10s of incubation, and is inhibited by PI3K inhibitors like seen in other studies, but also GPRC and PLC inhibitors; and when the cells are depleted of intra-cellular calcium Akt does not get phosphoraylized, and binding free calcium with EGTA lowered protein synthesis from 16% to 8%.  Calcium per se can be an important mediator of Akt and protein synthesis  , and ecdysteroids seem to work vicariously through Ca2+ and Akt.