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Post-translational modifications of PML: consequences and implications.

Cheng X, Kao HY - Front Oncol (2013)

Bottom Line: The tumor suppressor promyelocytic leukemia protein (PML) predominantly resides in a structurally distinct sub-nuclear domain called PML nuclear bodies.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.

View Article: PubMed Central - PubMed

Affiliation: 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.

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.

No MeSH data available.


Related in: MedlinePlus

Effects of extracellular stimuli on PML. A model summarizes stimuli that regulate PML modification and outcomes.
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Figure 4: Effects of extracellular stimuli on PML. A model summarizes stimuli that regulate PML modification and outcomes.

Mentions: Promyelocytic leukemia protein is post-translationally modified in response to different cellular stimuli (Figure 4). The different modifications form a complex regulatory network that modulates the activity of PML and PML NBs. It is clear that stimuli such as As2O3 and DNA damage induce both SUMOylation and phosphorylation of PML. The biggest challenge lies in the dissection of the biological effects of these modifications and the crosstalk among these modifications. The nature of low abundance or transient modification also serves as a barrier for this issue. However, the study and understanding of PML and PML NB-associated post-translational modifications will be necessary to establish its function at the molecular level.


Post-translational modifications of PML: consequences and implications.

Cheng X, Kao HY - Front Oncol (2013)

Effects of extracellular stimuli on PML. A model summarizes stimuli that regulate PML modification and outcomes.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3539660&req=5

Figure 4: Effects of extracellular stimuli on PML. A model summarizes stimuli that regulate PML modification and outcomes.
Mentions: Promyelocytic leukemia protein is post-translationally modified in response to different cellular stimuli (Figure 4). The different modifications form a complex regulatory network that modulates the activity of PML and PML NBs. It is clear that stimuli such as As2O3 and DNA damage induce both SUMOylation and phosphorylation of PML. The biggest challenge lies in the dissection of the biological effects of these modifications and the crosstalk among these modifications. The nature of low abundance or transient modification also serves as a barrier for this issue. However, the study and understanding of PML and PML NB-associated post-translational modifications will be necessary to establish its function at the molecular level.

Bottom Line: The tumor suppressor promyelocytic leukemia protein (PML) predominantly resides in a structurally distinct sub-nuclear domain called PML nuclear bodies.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.

View Article: PubMed Central - PubMed

Affiliation: 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.

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.

No MeSH data available.


Related in: MedlinePlus