Abstract

Significance BAP1 is a deubiquitinase of histone H2A involved in chromatin remodeling. Several studies identified BAP1 as major tumor suppressor inactivated in various cancers. Nonetheless, the manner in which BAP1 protects against cancer development remains enigmatic. We now show that BAP1 is recruited to double-strand DNA break sites and promotes error-free repair of these lesions. We also provide the first evidence that phosphorylation coordinates the function of BAP1 in promoting cellular recovery from DNA damage. Thus, our study represents a significant advance in the field of ubiquitin signaling in the context of cancer development.