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these findings uncover a novel mechanism by which PML loss may contribute to mTOR activation and cancer progression via dysregulation of basal DDIT4 gene expression.
This study establishes PML as an important regulator of NF-kappaB and demonstrates that PML-RARalpha dysregulates NF-kappaB.
STAT3 is responsible, at least in part, for the transcriptional upregulation of PML in breast cancer. Moreover, PML targeting hampers breast cancer initiation and metastatic seeding. Mechanistically, this biological activity relies on the regulation of the stem cell gene SOX9 through interaction of PML with its promoter region.
Respiratory syncytial virus induces NRF2 degradation through a PML-RNF4 pathway.
Data suggest that intracellular host defenses are counteracted by ICP0, which targets PML for degradation from the outset of nuclear infection to promote viral-DNA release from PML-nuclear bodies and the onset of HSV-1 lytic replication. (ICP0 = immediate early infected polypeptide-0; PML = promyelocytic leukemia protein; HSV-1 = herpes simplex virus-1)
the PML(NLS-) protein was detectable in the cytoplasm of neutrophils from patients with acute promyelocytic leukemia.
The PML sumo interaction motif differentially affects nuclear body formation by each individual isoform.
inhibiting CK2 can enhance sensitivity of Cisplatin to Non-small cell lung carcinoma cells through PML
Results show that PolySUMO5 conjugation on K160 of PML results in recruitment of proteins to form PML-nuclear bodies. SUMO5 conjugation on PML is gradually replaced by SUMO2/3 conjugation, which leads to RNF4-mediated disruption of PML-NBs.
the ND10 bodies become viral replication compartments, and ICP0, a viral E3 ligase, degrades both PML and SP100. The amounts of PML and SP100 and the number of ND10 structures increase in cells exposed to IFN-beta.
These results therefore indicate that EGCG targets PML/RARalpha oncoprotein for degradation and potentiates differentiation of promyelocytic leukemia cells in combination with ATRA via PTEN.
Mechanically, mutant NPM1 interacted with PML and mediated its delocalization as well as stabilization contributing to elevated autophagic activity and leukemic cell survival in vitro.
study revealed molecular mechanism of responsiveness of the PML-RARA mutations to AS2O3 treatment; mutation S214L disrupted PML-arsenic binding, nuclear body formation, basal SUMOylation and degradation; mutation A216T showed moderate defect in AS2O3 response;, mutants L217F and S220G behave similarly to wild-type; findings suggest distinct mutants of PML-RARA confer varying degree of AS2O3 resistance
Silencing of PML-RAR and RARalpha2 results in similar increases in the constitutive expression of several granulocytic differentiation markers.
Our findings unveil a novel essential oncogenic activity of PML/RARA in Acute promyelocitic leukemia
Findings reveal a previously unrecognized role of c-Myc as a potential ceRNA for PML/RARalpha in acute promyelocytic leukemia.
PML loss promotes tumor development, providing a growth advantage to tumor cells that use autophagy as a cell survival strategy during stress conditions.
WDR4 is an oncoprotein that negatively regulates PML via ubiquitination to promote lung cancer progression by fostering an immunosuppressive and prometastatic tumor microenvironment
Sumoylation of PML with SUMO2 by UBC9/UBE2I can lead to formation of polymeric SUMO chains. Data suggest that coordination of growing poly-SUMO chain with "back side" binding site on UBC9/UBE2I appears to be required for SUMO chain elongation on PML. (PML = promyelocytic leukemia protein; SUMO2 = small ubiquitin-like modifier 2; UBC9/UBE2I = ubiquitin-conjugating enzyme UBC9/UBE2I)
Data show that the cytoplasmic localization of promyelocytic leukaemia (PML) is mediated by its nuclear export in a chromosomal maintenance 1 (CRM1)-dependent manner.
PML mediates the binding of PER2 to BMAL1 in the BMAL1/CLOCK heterodimer and is an important component in the organization of a functional clock complex in the nucleus.
Promyelocytic leukemia protein Pml -/- cells showed a higher proliferation rate, compared to Pml +/+ cells.
PML protein organizes heterochromatin domains where it regulates histone H3.3 deposition by ATRX and DAXX.
Data indicate that promyelocytic leukemia protein knockout (Pml-/-) animals fail to properly activate oxidative stress-responsive p53 targets, whereas the NRF2 response is amplified and accelerated.
data support a model in which activation of myogenic differentiation results in PML NB loss, chromatin reorganization and DAXX relocalization, and provides a paradigm for understanding the consequence of PML loss in other cellular contexts, such as during cancer development and progression
a regulatory role of ZNF451-1 in fine-tuning physiological PML levels
The data demonstrate a dual role of PML in protection and recovery after brain injury.
This study designates PML protein and PML-NBs to be major cellular components involved in the control of Herpes simplex virus 1 (HSV-1) latency, probably during the entire life of an individual.
Study found that Promyelocytic leukemia protein (PML) is broadly expressed across the gray matter, with the highest levels in the cerebral and cerebellar cortices. PML bodies are broadly involved in activity-dependent nuclear phenomena in adult neurons
These findings suggest that the UBC9/PML/RNF4 axis plays a critical role as an important SUMO pathway in cardiac fibrosis. Modulating the protein levels of the pathway provides an attractive therapeutic target for the treatment of cardiac fibrosis and heart failure.
PML contributes to the intrinsic restriction of HIV-1 infections in a cell type-dependent manner.
both the PML-RARA-driven competitive transplantation advantage and development of acute promyelocytic leukemia (APL) required DNMT3A
PML IV enhances global SUMO-1 conjugation, particularly that of p53, resulting in p53 stabilization and activation.
our findings challenge the predominant model in the field and we propose that PML/RARA initiates leukemia by subtly shifting cell fate decisions within the promyelocyte compartment.
DNA-binding-defective PML/RARA mutants could not repress the transcription of retinoic acid regulated genes.
A novel antioxidative mechanism by which PML regulates cellular oxidant homeostasis by controlling complex II integrity and Nrf2 activity and identified PML as an indispensable mediator of SFN activity.
pRB can interact with PML specifically during senescence, suggesting that signaling events in senescence regulate assembly of PML and pRB to establish heterochromatin and create a permanent cell cycle arrest.
Data suggest that acute promyelocytic leukemia (APL) differentiation is a default program triggered by clearance of promyelocytic leukemia-retinoic acid receptor alpha fusion oncoprotein PML/RARA-bound promoters.
Our results add PML/TRIM19 to the growing list of TRIM proteins implicated in both intrinsic and innate immunity.
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This phosphoprotein localizes to nuclear bodies where it functions as a transcription factor and tumor suppressor. Its expression is cell-cycle related and it regulates the p53 response to oncogenic signals. The gene is often involved in the translocation with the retinoic acid receptor alpha gene associated with acute promyelocytic leukemia (APL). Extensive alternative splicing of this gene results in several variations of the protein's central and C-terminal regions\; all variants encode the same N-terminus. Alternatively spliced transcript variants encoding different isoforms have been identified.
RING finger protein 71
, probable transcription factor PML
, promyelocytic leukemia protein
, promyelocytic leukemia, inducer of
, protein PML
, tripartite motif protein TRIM19
, tripartite motif-containing protein 19
, promyelocytic leukemia
, probable transcription factor PML-like