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Incoming human papillomavirus 16 genome is lost in PML protein-deficient HACAT keratinocytes.

ABSTRACT: Human papillomaviruses (HPVs) target PML nuclear bodies during infectious entry and PML protein is important for efficient transcription of incoming viral genome.We used shRNA to knockdown PML protein in HaCaT keratinocytes to further investigate the role of PML protein in HPV entry. We used microarrays to compare the transcriptome of PML protein-deficient with vector control-transduced HaCaT cells.

ORGANISM(S): Homo sapiens

PROVIDER: GSE89937 | GEO | 2016/11/17

SECONDARY ACCESSION(S): PRJNA354288

REPOSITORIES: GEO

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Homo sapiens

Project description:Incoming human papillomavirus 16 genome is lost in PML protein-deficient HACAT keratinocytes.

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PML regulates NF-ÎºB phosphorylation and transcriptional activity

Project description:The transcription factor NF-ÎºB is considered the master regulator of the immune response but also acts broadly to regulate gene expression that influences cell survival, proliferation and differentiation. Post-translational modification of NF-ÎºB, phosphorylation in particular, is essential for the transactivation activity of NF-ÎºB. Emerging evidence suggests that the regulation of NF-ÎºB in the nucleus is critical in controlling gene expression. Promyelocytic Leukemia (PML) is a nuclear protein that forms nuclear bodies (PML NBs), sub-nuclear structures that are associated with transcriptionally active genomic regions that have been implicated in multiple processes such as apoptosis, senescence and anti-viral responses. Chromosomal translocations leading to the expression of a PML-retinoic acid receptor-Î± (PML-RARÎ±) fusion protein are causative for acute promyelocytic leukemia (APL) characterised by a differentiation block at the promyelocytic state of myeloid development. Here we demonstrate that PML is required for phosphorylation of NF-ÎºB p65 and that PML is essential for NF-ÎºB- induced transcriptional responses. Our analysis of available transcriptional profiles of all-trans retinoic acid treated acute promyelocytic leukemia (APL) cells identifies a NF-ÎºB transcriptional programme suppressed by PML-RARÎ±. We further demonstrate that PML-RARÎ± inhibits NF-ÎºB phosphorylation and transcriptional activity. Our findings demonstrate a critical role for PML in promoting NF-ÎºB transcriptional activity which may contribute to APL initiation and maintenance. WT and PML-/- MEFs were analysed for gene expression analysis. Total of 12 samples, inlcluding triplicates were utilized. WT MEFs and PML-/- were stimulated with TNFÎ± for three hours and analysed for gene expresison using unstimulated WT MEFs as control.

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Gene expression profiling of Pml wt and Pml KO mice liver after fasted 6h

Project description:The Pml gene is essential to the formation of PML nuclear bodies, domains which have been associated with various functions such as apoptosis/senescence, DNA repair and cell proliferation( Lallemand-Breitenbach 2010). PML-NBs formation is regulated by cellular stress including oxidative stress(Jeanne 2010, de The 2012). To investigate the role of PML in ROS response in vivo, we analyse the expression difference betweem Pml wt and Pml KO under fasted condition, which easily up-regulate ROS in BALB/cByJ background

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Identification of downstream targets of the human papillomavirus E6 and E7 oncoproteins by RNA interference

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PML regulates NF-κB transcriptional activity

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2016-06-01 | GSE47828 | GEO

The Sp100 component of ND10/PML bodies is a potent tumor suppressor

Project description:Identifying the functions of proteins, which define specific subnuclear structures and territories, is important for understanding eukaryotic nuclear dynamics. Sp100 is a prototypical protein of ND10/PML bodies and co-localizes with the proto-oncogenic protein PML and Daxx, proteins with critical roles in oncogenic transformation, interferon-mediated viral resistance and response to PML-directed cancer therapeutics. Sp100 isoforms contain PHD, Bromo and HMG domains and are highly sumoylated at ND10/PML bodies, all characteristics suggestive of a role in chromatin mediated gene regulation. However, no clear role for the Sp100 component of PML bodies in oncogenesis has been defined. Using isoform-specific knockdown techniques, we show that most human diploid fibroblasts, which lack Sp100, rapidly senesce and discuss gene expression changes associated with this rapid senescence.

2012-12-04 | GSE20613 | GEO

Identification of potential human PML interacting proteins in Nicotiana benthamiana

Project description:In spite of the crucial tasks fulfilled by the subnuclear structures known as PML nuclear bodies (PML-NBs) in mammalian cells, the presence of PML-NBs in plant cells could not be shown yet. Interestingly, the key organizer of PML-NBs, human promyelocytic leukemia protein (PML), is not targeted to structures resembling PML-NBs when expressed heterologously in plants, but localizes to interchromosomal areas associated with the nucleolus. In order to identify plant proteins interacting with human PML, a GFP-fusion protein was ectopically expressed in Nicotiana benthamiana using Agrobacterium tumefaciens mediated transformation. The bait protein as well as potential interactors were immunoprecipitated by use of magnetic GFP-Trap beads (Chromotek). Precipitated proteins were analyzed by Nano-LC-MS/MS.

2016-10-10 | PXD004254 | Pride

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