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WDR4 (show WDR4 Proteins) 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 (show SUMO2 Proteins) by UBC9/UBE2I (show UBE2I Proteins) 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 (show UBE2I Proteins) appears to be required for SUMO chain elongation on PML. (PML = promyelocytic leukemia protein; SUMO2 (show SUMO2 Proteins) = small ubiquitin-like modifier 2 (show SUMO2 Proteins); UBC9/UBE2I (show UBE2I Proteins) = ubiquitin-conjugating enzyme (show Ube2t Proteins) UBC9/UBE2I (show UBE2I Proteins))
Data show that the cytoplasmic localization of promyelocytic leukaemia (PML) is mediated by its nuclear export in a chromosomal maintenance 1 (CRM1 (show XPO1 Proteins))-dependent manner.
this study, we first observed that PML-positive intranuclear aggregates also appeared in controls and were not specific for the Neuronal Intranuclear Hyaline Inclusion Disease cases.
TRIB3 (show TRIB3 Proteins) promotes acute promyelocytic leukemia progression through stabilization of the oncoprotein PML-RARalpha (show RARA Proteins) and inhibition of p53 (show TP53 Proteins)-mediated senescence.
Data suggest that the binding of Z-10 to RXRalpha (show RXRA Proteins) inhibited the interaction of RXRalpha (show RXRA Proteins) with PML-RARalpha (show RARA Proteins), leading to Z-10's selective induction of PML-RARalpha (show RARA Proteins) degradation.
PML protein prevents the loss of HPV genome following infection implying that the host cell may be able to recognize chromatinized HPV genome or the associated capsid proteins.
findings demonstrate that the PML protein, which mediates an intrinsic immune response against human cytomegalovirus, specifically serves as an E3 ligase for SUMO modification of IE1p72.
During infection, PML undergoes oxidation-mediated multimerization, associates with the nuclear matrix, and becomes de-SUMOylated due to the pore-forming activity of the Listeria toxin listeriolysin O (LLO).
Data suggest PML (promyelocytic leukemia protein) positively regulates STAT1 (show STAT1 Proteins) and STAT2 (show STAT2 Proteins) isgylation, a ubiquitination-like protein modification; PML exhibits potent angiostatic activity, doing so in part by forming a positive feedforward loop with STAT1 (show STAT1 Proteins)/2 and a negative feedback loop with STAT3 (show STAT3 Proteins). (STAT (show STAT1 Proteins) = signal transducer and activator of transcription (show STAT1 Proteins))
The data demonstrate a dual role of PML in protection and recovery after brain injury.
This study designates PML protein and PML-NBs (show NLRP2 Proteins) 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 (show RARA Proteins)-driven competitive transplantation advantage and development of acute promyelocytic leukemia (APL (show FASL Proteins)) required DNMT3A (show DNMT3A Proteins)
PML IV enhances global SUMO-1 (show SUMO1 Proteins) conjugation, particularly that of p53 (show TP53 Proteins), resulting in p53 (show TP53 Proteins) stabilization and activation.
our findings challenge the predominant model in the field and we propose that PML/RARA (show RARA Proteins) initiates leukemia by subtly shifting cell fate decisions within the promyelocyte compartment.
DNA-binding-defective PML/RARA (show RARA Proteins) 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 (show NFE2L2 Proteins) activity and identified PML as an indispensable mediator of SFN (show SFN Proteins) activity.
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.
, probable transcription factor PML
, promyelocytic leukemia protein
, protein PML
, probable transcription factor PML-like
, RING finger protein 71
, promyelocytic leukemia, inducer of
, tripartite motif protein TRIM19
, tripartite motif-containing protein 19