Researchers from University of California, San Diego have identified an enzyme that controls the spread of breast cancer. This finding was reported in PNAS and offer new insights of understanding the metastasis of breast cancer.

Breast cancer is the leading invasive cancer among women worldwide. Its metastatic recurrence can happen many years after the removal of the primary tumor and cause the mortality. The current treatments ,including surgical removal and localized radiotherapy, are effective against primary Breast cancer, but could do little to prevent metastatic recurrence. Even Chemotherapy is not helpful to prevent metastatic recurrence.

In this study, researchers have demonstrated an ubiquitin conjugating enzyme Ubc13, which could catalyze K63-linked protein polyubiquitination, is largely dispensable for primary mammary tumor growth but is required for metastatic spread and lung colonization by Breast cancer cells. Ubc13 is required for TGFβ-induced non-SMAD signaling via TAK1 and p38, a pathway that is first activated in the primary tumor. The study has identified an Ucb13- and p38-dependent metastatic gene signature , explaining how p38 may control metastasis and providing a measure for monitoring the effectiveness of pharmacologic p38 inhibition, which inhibits the growth of established metastatic lesions. It suggests that p38 inhibition should be considered as a potential treatment for metastatic breast cancer.

Reference:

 Wu, X., Zhang, W., Font-Burgada, J., Palmer, T., Hamil, A. S., Biswas, S. K., … & Karin, M. (2014). Ubiquitin-conjugating enzyme Ubc13 controls breast cancer metastasis through a TAK1-p38 MAP kinase cascade.Proceedings of the National Academy of Sciences, 201414358.