BubR1 is a putative serine-threonine protein kinase with a variety of critical cellular functions, most of which are largely mitotic. BubR1, which is a regulator of genomic integrity, may lie at the interface of aging and cancer. While it has been long known that aging is a key contributor to disease, exploration of the molecular basis of the interrelationship between aging and disease has made notable progress over the past two decades. Understanding the molecular mechanisms promoting these modifications and their roles in regulating BubR1 is important for our current understanding and future studies of BubR1 in maintaining genomic integrity as well as in aging and cancer.Īging is one of the greatest risk factors for the development of a variety of diseases, including cancer. In this review, we discuss the currently characterized post-translational modifications to BubR1, the enzymes involved, and the biological consequences to BubR1 functionality and implications in diseases associated with BubR1. Post-translational modifications, including but not limited to phosphorylation, acetylation, and ubiquitination, play a critical role in the temporal and spatial regulation of BubR1 function. BubR1 is also progressively downregulated with age and has been shown to be directly involved in the aging process through suppression of cellular senescence. Loss or mutation of BubR1 results in aneuploidy that precedes various potential pathologies, including cancer and mosaic variegated aneuploidy (MVA). BubR1 is an essential component of the spindle assembly checkpoint (SAC) during mitosis where it functions to prevent anaphase onset to ensure proper chromosome alignment and kinetochore-microtubule attachment.

Spindle assembly checkpoint