title: Post-translational modifications of PML: consequences and implications.
abstract: The tumor suppressor promyelocytic leukemia protein (PML) predominantly resides in a structurally distinct sub-nuclear domain called PML nuclear bodies. Emerging evidences indicated that PML actively participates in many aspects of cellular processes, but the molecular mechanisms underlying PML regulation in response to stress and environmental cues are not complete. Post-translational modifications, such as SUMOylation, phosphorylation, acetylation, and ubiquitination of PML add a complex layer of regulation to the physiological function of PML. In this review, we discuss the fast-moving horizon of post-translational modifications targeting PML.
authors: Department of Biochemistry, School of Medicine, Case Western Reserve University Cleveland, OH, USA ; Comprehensive Cancer Center, Case Western Reserve University Cleveland, OH, USA ; University Hospital of Cleveland, Case Western Reserve University Cleveland, OH, USA.
authors: Xiwen
authors: X
authors: Cheng
authors: Hung-Ying
authors: HY
authors: Kao
keywords: PML; SUMOylation; acetylation; phosphorylation; post-translational modification; review; sumo