PR55α subunit of protein phosphatase 2A supports KRAS-driven tumorigenesis that requires YAP activation.

PP2A holoenzymes account nearly 50% of Ser/Thr phosphatase activities in human cells, yet their roles in oncogenesis remain largely unexplored. A PP2A holoenzyme consists of a catalytic subunit, a scaffold subunit, and a regulatory subunit. We previously reported that PR55α, a PP2A regulatory subunit, supports the tumorigenic and metastatic potential of pancreatic cancer cells, and this is associated with its role in promoting YAP activation, which is essential for tumorigenesis and progression in most solid tumors, including pancreatic cancer.

PR55α-controlled protein phosphatase 2A inhibits p16 expression and blocks cellular senescence induction by γ-irradiation.

Cellular senescence is a permanent cell cycle arrest that can be triggered by both internal and external genotoxic stressors, such as telomere dysfunction and DNA damage. The execution of senescence is mainly by two pathways, p16/RB and p53/p21, which lead to CDK4/6 inhibition and RB activation to block cell cycle progression. While the regulation of p53/p21 signaling in response to DNA damage and other insults is well-defined, the regulation of the p16/RB pathway in response to various stressors remains poorly understood.

Benzimidazole carbamate induces cytotoxicity in breast cancer cells via two distinct cell death mechanisms.

Metastatic breast cancer (mBC) is responsible for >90% of breast cancer-related deaths. Microtubule-targeting agents (MTAs) are the front-line treatment for mBC. However, the effectiveness of MTAs is frequently limited by the primary or acquired resistance.