This labeling strategy was applied to clarify mechanistic features of the ubiquitin E3 ligase WWP2 including its interaction with one of its substrates, the tumor suppressor PTEN, as well as its autoubiquitination molecularity.
Our results demonstrate that WWP2, rather than CHIP, is an ubiquitin ligase that promotes PTEN degradation <i>in vivo</i> Considering PTEN's significant role in tumor development, we propose that WWP2 may be a potential target for fine-tuning PTEN levels in anticancer therapies.
We found that WWP2 expression was elevated in lung adenocarcinoma tissues and was correlated with the tumor differentiation stage, TNM stage and presence of lymph node metastasis.
We detected a strong WWP2 expression in tumor tissues of the People's Hospital of Lishui, and the survival rate was significantly higher in patients with lower WWP2-expressing tumors.
Furthermore, WWP2 isoforms have been shown to selectively target oncogenic signaling pathways linked to both the pTEN tumour suppressor and the TGFβ/Smad signaling pathway.