SMAD specific E3 ubiquitin protein ligase 1 promotes ovarian cancer cell migration and invasion via the activation of the RhoA/ROCK signaling pathway

SMAD specific E3 ubiquitin protein ligase 1 (SMURF1) serves a pivotal role in a variety of pathological processes and in tumor cell migration and invasion; however, its functional mechanism in ovarian cancer (OC) remains unknown. Previously, we observed overexpression of SMURF1 in OC tissues. In the present study, the role of SMURF1 in OC metastasis was investigated. The results revealed that SMURF1 was upregulated in OC cell lines of greater aggression than less aggressive cells. Downregulation of SMURF1 significantly inhibited OC cell invasion and migration, whereas upregulation of SMURF1 promoted OC cell invasion and migration. Investigation of the mechanism underlying the effects of SMURF1 in OC revealed that SMURF1 induced OC cell migration and invasion via activation of the Ras homolog family member A/Rho-associated protein kinase signaling pathway. Further analysis demonstrated that higher levels of SMURF1 expression were associated with shorter overall survival in patients with OC. The findings of the present study indicated that overexpression of SMURF1 may contribute to the malignancy and metastasis of OC. The inhibition of SMURF1 expression may be a promising strategy for the treatment of patients with OC.