Open AccessPML nuclear body biogenesis and oligomerization-driven leukemogenesis
Author(s) -
Yuwen Li,
Xiaodan Ma,
Guoyu Meng
Publication year - 2020
Publication title -
blood science
Language(s) - English
Resource type - Journals
ISSN - 2543-6368
DOI - 10.1097/bs9.0000000000000034
Subject(s) - promyelocytic leukemia protein , sumo protein , biogenesis , acute promyelocytic leukemia , microbiology and biotechnology , nuclear protein , chemistry , cancer research , biology , ubiquitin , biochemistry , transcription factor , retinoic acid , gene
PML nuclear bodies (NBs), which are increasingly recognized as the central hub of many cellular signaling events, are superassembled spherical complexes with diameters of 0.1-2 μm. Recent studies reveal that RING tetramerization and B1-box polymerization are key factors to the overall PML NBs assembly. The productive RBCC oligomerization allows subsequent PML biogenesis steps, including the PML auto-sumoylation and partners recruitment via SUMO-SIM interactions. In promyelocytic leukemia, the oncoprotein PML/RARα (P/R) inhibits PML NBs assembly and leads to a full-fledged leukemogenesis. In this review, we review the recent progress in PML and acute promyelocytic leukemia fields, highlighting the protein oligomerization as an important direction of future targeted therapy.