TY - JOUR
T1 - Post-translational modifications of PML
T2 - Consequences and implications
AU - Cheng, Xiwen
AU - Kao, Hung Ying
PY - 2013
Y1 - 2013
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84885626870&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84885626870&partnerID=8YFLogxK
U2 - 10.3389/fonc.2012.00210
DO - 10.3389/fonc.2012.00210
M3 - Review article
AN - SCOPUS:84885626870
SN - 2234-943X
VL - 2 JAN
JO - Frontiers in Oncology
JF - Frontiers in Oncology
M1 - Article 00210
ER -