scholarly journals C-terminal motifs in promyelocytic leukemia protein isoforms critically regulate PML nuclear body formation

2017 ◽  
Vol 130 (20) ◽  
pp. 3496-3506 ◽  
Author(s):  
Chuang Li ◽  
Qiongfang Peng ◽  
Xiao Wan ◽  
Haili Sun ◽  
Jun Tang
Keyword(s):  
Nuclear Body ◽  
Promyelocytic Leukemia ◽  
Protein Isoforms ◽  
Promyelocytic Leukemia Protein ◽  
Body Formation

scholarly journals Contribution of the C-terminal Regions of Promyelocytic Leukemia Protein (PML) Isoforms II and V to PML Nuclear Body Formation

2012 ◽  
Vol 287 (36) ◽  
pp. 30729-30742 ◽  
Author(s):  
Yunyun Geng ◽  
Shamci Monajembashi ◽  
Anwen Shao ◽  
Di Cui ◽  
Weiyong He ◽  
...  
Keyword(s):  
Nuclear Body ◽  
Promyelocytic Leukemia ◽  
Promyelocytic Leukemia Protein ◽  
Body Formation

scholarly journals A novel GTPase, CRAG, mediates promyelocytic leukemia protein–associated nuclear body formation and degradation of expanded polyglutamine protein

2006 ◽  
Vol 172 (4) ◽  
pp. 497-504 ◽  
Author(s):  
Qingyu Qin ◽  
Ryoko Inatome ◽  
Azusa Hotta ◽  
Masaki Kojima ◽  
Hirohei Yamamura ◽  
...  
Keyword(s):  
Nuclear Translocation ◽  
Nuclear Body ◽  
Promyelocytic Leukemia ◽  
Dependent Manner ◽  
Polyglutamine Diseases ◽  
Promyelocytic Leukemia Protein ◽  
Localization Signal ◽  
Guanosine Triphosphatase ◽  
Interfering Rna ◽  
Polyglutamine Protein

Polyglutamine diseases are inherited neurodegenerative diseases caused by the expanded polyglutamine proteins (polyQs). We have identified a novel guanosine triphosphatase (GTPase) named CRAG that contains a nuclear localization signal (NLS) sequence and forms nuclear inclusions in response to stress. After ultraviolet irradiation, CRAG interacted with and induced an enlarged ring-like structure of promyelocytic leukemia protein (PML) body in a GTPase-dependent manner. Reactive oxygen species (ROS) generated by polyQ accumulation triggered the association of CRAG with polyQ and the nuclear translocation of the CRAG–polyQ complex. Furthermore, CRAG promoted the degradation of polyQ at PML/CRAG bodies through the ubiquitin–proteasome pathway. CRAG knockdown by small interfering RNA in neuronal cells consistently blocked the nuclear translocation of polyQ and enhanced polyQ-mediated cell death. We propose that CRAG is a modulator of PML function and dynamics in ROS signaling and is protectively involved in the pathogenesis of polyglutamine diseases.

scholarly journals Promyelocytic Leukemia Protein (Pml) and Daxx Participate in a Novel Nuclear Pathway for Apoptosis

2000 ◽  
Vol 191 (4) ◽  
pp. 631-640 ◽  
Author(s):  
Sue Zhong ◽  
Paolo Salomoni ◽  
Simona Ronchetti ◽  
Ailan Guo ◽  
Davide Ruggero ◽  
...  
Keyword(s):  
Acid Treatment ◽  
Nuclear Body ◽  
Promyelocytic Leukemia ◽  
Retinoic Acid Treatment ◽  
Promyelocytic Leukemia Protein ◽  
Disease Remission ◽  
Activation Induced Cell Death ◽  
A Cell ◽  
Dependent Pathway

The promyelocytic leukemia protein (PML) gene of acute promyelocytic leukemia (APL) encodes a cell growth and tumor suppressor essential for multiple apoptotic signals. Daxx was identified as a molecule important for the cytoplasmic transduction of the Fas proapoptotic stimulus. Here, we show that upon mitogenic activation of mature splenic lymphocytes, Daxx is dramatically upregulated and accumulates in the PML nuclear body (NB) where PML and Daxx physically interact. In the absence of PML, Daxx acquires a dispersed nuclear pattern, and activation-induced cell death of splenocytes is profoundly impaired. PML inactivation results in the complete abrogation of the Daxx proapoptotic ability. In APL cells, Daxx is delocalized from the NB. Upon retinoic acid treatment, which induces disease remission in APL, Daxx relocalizes to the PML NBs. These results indicate that PML and Daxx cooperate in a novel NB-dependent pathway for apoptosis and shed new light in the role of PML in tumor suppression.

Role of SUMO-1–modified PML in nuclear body formation

Blood ◽  
2000 ◽  
Vol 95 (9) ◽  
pp. 2748-2752 ◽  
Author(s):  
Sue Zhong ◽  
Stefan Müller ◽  
Simona Ronchetti ◽  
Paul S. Freemont ◽  
Anne Dejean ◽  
...  
Keyword(s):  
Nuclear Localization ◽  
Critical Role ◽  
Nuclear Body ◽  
Promyelocytic Leukemia ◽  
Nuclear Bodies ◽  
Localization Pattern ◽  
Body Formation ◽  
Functional Relevance ◽  
Do So

The tumor-suppressive promyelocytic leukemia (PML) protein of acute promyelocytic leukemia (APL) has served as one of the defining components of a class of distinctive nuclear bodies (NBs). PML is delocalized from NBs in APL cells and is degraded in cells infected by several viruses. In these cells, NBs are disrupted, leading to the aberrant localization of NB proteins. These results have suggested a critical role for the NB in immune response and tumor suppression and raised the question of whether PML is crucial for the formation or stability of NB. In addition, PML is, among other proteins, covalently modified by SUMO-1. However, the functional relevance of this modification is unclear. Here, we show in primary PML−/− cells of various histologic origins, that in the absence of PML, several NB proteins such as Sp100, CBP, ISG20, Daxx, and SUMO-1 fail to accumulate in the NB and acquire aberrant localization patterns. Transfection of PML in PML−/−cells causes the relocalization of NB proteins. By contrast, a PML mutant that can no longer be modified by SUMO-1 fails to do so and displays an aberrant nuclear localization pattern. Therefore, PML is required for the proper formation of the NB. Conjugation to SUMO-1 is a prerequisite for PML to exert this function. These data shed new light on both the mechanisms underlying the formation of the NBs and the pathogenesis of APL.

scholarly journals Promyelocytic leukemia-nuclear body formation is an early event leading to retinoic acid-induced differentiation of neuroblastoma cells

2007 ◽  
Vol 0 (0) ◽  
pp. 071106220615005-???
Author(s):  
A. Delaune ◽  
C. Corbière ◽  
F. D Benjelloun ◽  
E. Legrand ◽  
J. P. Vannier ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Neuroblastoma Cells ◽  
Nuclear Body ◽  
Promyelocytic Leukemia ◽  
Early Event ◽  
Induced Differentiation ◽  
Body Formation

scholarly journals Resistance to Virus Infection Conferred by the Interferon-Induced Promyelocytic Leukemia Protein

1998 ◽  
Vol 72 (2) ◽  
pp. 1043-1051 ◽  
Author(s):  
Mounira K. Chelbi-Alix ◽  
Frédérique Quignon ◽  
Luis Pelicano ◽  
Marcel H. M. Koken ◽  
Hugues de Thé
Keyword(s):  
Influenza A ◽  
Coiled Coil ◽  
Antiviral Effect ◽  
Nuclear Body ◽  
Promyelocytic Leukemia ◽  
Nuclear Bodies ◽  
Encephalomyocarditis Virus ◽  
Promyelocytic Leukemia Protein ◽  
Associated Proteins ◽  
Vesicular Stomatitis

ABSTRACT The interferon (IFN)-induced promyelocytic leukemia (PML) protein is specifically associated with nuclear bodies (NBs) whose functions are yet unknown. Two of the NB-associated proteins, PML and Sp100, are induced by IFN. Here we show that overexpression of PML and not Sp100 induces resistance to infections by vesicular stomatitis virus (VSV) (a rhabdovirus) and influenza A virus (an orthomyxovirus) but not by encephalomyocarditis virus (a picornavirus). Inhibition of viral multiplication was dependent on both the level of PML expression and the multiplicity of infection and reached 100-fold. PML was shown to interfere with VSV mRNA and protein synthesis. Compared to the IFN mediator MxA protein, PML had less powerful antiviral activity. While nuclear body localization of PML did not seem to be required for the antiviral effect, deletion of the PML coiled-coil domain completely abolished it. Taken together, these results suggest that PML can contribute to the antiviral state induced in IFN-treated cells.

scholarly journals Nuclear body phase separation drives telomere clustering in ALT cancer cells

2020 ◽  
Vol 31 (18) ◽  
pp. 2048-2056 ◽  
Author(s):  
Huaiying Zhang ◽  
Rongwei Zhao ◽  
Jason Tones ◽  
Michel Liu ◽  
Robert L. Dilley ◽  
...  
Keyword(s):  
Dna Repair ◽  
Phase Separation ◽  
Cancer Cells ◽  
Nuclear Body ◽  
Promyelocytic Leukemia ◽  
Nuclear Bodies ◽  
Telomere Elongation ◽  
Alternative Lengthening ◽  
Induce Phase Separation ◽  
Induce Phase

A chemical dimerization approach is developed to induce phase separation of APB nuclear bodies involved in telomere elongation in alternative lengthening of telomeres (ALT) cancer cells. It reveals that ALT telomere-associated promyelocytic leukemia nuclear body (APB) fusion leads to telomere clustering to provide templates for homology-directed telomere synthesis, an ability that is decoupled from APB function in enriching DNA repair factors.

M33 condenses chromatin through nuclear body formation and methylation of both histone H3 lysine 9 and lysine 27

2021 ◽  
pp. 119100
Author(s):  
Yu-Ru Lin ◽  
You-Yu Liu ◽  
Hsin-Chi Lan ◽  
Chiung-Chyi Shen ◽  
Ya-Li Yao ◽  
...  
Keyword(s):  
Histone H3 ◽  
Nuclear Body ◽  
Body Formation

scholarly journals Loss of the Promyelocytic Leukemia Protein in Gastric Cancer: Implications for IP-10 Expression and Tumor-Infiltrating Lymphocytes

PLoS ONE ◽  
2011 ◽  
Vol 6 (10) ◽  
pp. e26264 ◽  
Author(s):  
Hee Ja Kim ◽  
Dong Eun Song ◽  
Seul Ye Lim ◽  
Sung-Hee Lee ◽  
Jihee Lee Kang ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Tumor Infiltrating Lymphocytes ◽  
Promyelocytic Leukemia ◽  
Promyelocytic Leukemia Protein ◽  
Infiltrating Lymphocytes
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