Regulation of XXXX stability as a consequence of DNA damage.

@entity5 @entity7465 @entity105 @entity876
UNASSIGNED: Cells in our body are constantly exposed to various stresses and threats to their genomic integrity. The @entity5 suppressor protein @entity876 plays a critical role in successful defense against these threats by inducing apoptotic cell death or cell cycle arrest. In unstressed conditions, @entity876 levels and activity must be kept low to prevent lethal activation of apoptotic and senescence pathways. However, upon DNA damage or other stressors, @entity876 is released from its inhibitory state to induce an array of apoptosis and cell cycle genes. Conversely, inactivation of @entity876 could promote unrestrained @entity5 proliferation and failure to appropriately undergo apoptotic cell death, which could, in turn, lead to @entity105 . The ubiquitin E3 ligase @entity7465 is the most critical inhibitor of @entity876 that determines the cellular response to various @entity876 -activating agents, including DNA damage. @entity7465 activity is controlled by post-translational modifications, especially phosphorylation. However, accumulating evidence suggests that @entity7465 is also regulated at the level of protein stability, which is controlled by the ubiquitin-proteasome pathway. Here, we discuss how @entity7465 can be regulated in response to DNA damage with particular focus on the regulation of @entity7465 protein stability. This article is protected by copyright. All rights reserved.
