WWP2 (E8W8A) Rabbit mAb #41182

Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26S proteasome. Ubiquitin is first activated by forming a thiolester complex with the activation component E1. The activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2, and then from E2 to ubiquitin ligase E3 for final delivery to the ε-NH₂ of the target protein lysine residue (1-3). Research studies suggest that activated E2 associates transiently with E3, and the dissociation is a critical step for ubiquitination (4).

WWP2 (WW domain-containing protein 2, AIP2) is a member of the NEDD4 family of E3 ligases, which play an important role in protein ubiquitination. WWP2 may play a role in multiple processes, including chondrogenesis and oncogenic signaling pathway regulation via interactions with Smad proteins and the tumor suppressor PTEN. It has recently become clear that aberrant activity of WWP2 may play a role in multiple tumor types and promotes tumorigenesis through the PTEN/Akt signaling pathway. Recently, accumulating evidence indicates that WWP2 plays a crucial part in the pathogenesis of different tumor types (5).