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Validated All-in-One™ qPCR Primer for PML(NM_033238.3) Search again
Product ID:
HQP158881
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
MYL, PP8675, RNF71, TRIM19
Gene Description:
PML nuclear body scaffold
Target Gene Accession:
NM_033238.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
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. [provided by RefSeq].
Gene References into function
- UBE1L is a retinoid target that triggers PML/RARalpha degradation and apoptosis in acute promyelocytic leukemia
- contributes to innate immunity, defining host susceptibility to viral infections and immunopathology
- antagonized by SIR2
- variant-type PML-RAR(alpha) fusion transcript in acute promyelocytic leukemia
- Promyelocytic leukemia protein PML inhibits Nur77-mediated transcription through specific functional interactions.
- induced PML in a mouse model
- represses A20-mediated transcription.
- Of seven known PML isoforms, only PML IV is capable of causing premature senescence in PML +/+ murine and human primary fibroblasts but not in PML -/- murine cells, providing the first evidence for functional differences among these isoforms.
- PML is a key stress-responsive regulator of eIF4E mRNA-dependent transport. PML inhibition of eIF4E depends on its association with the eIF4E nuclear body.
- PML does not affect herpes simplex virus 1 replication or the changes in the localization of ICP0 through infection
- PML is a target gene of beta-catenin and plakoglobin, and coactivates beta-catenin-mediated transcription.
- PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2
- SUMO-1 protease-1 regulates gene transcription through PML
- Purified RINGs, including PML, self-assemble into supramolecular structures in vitro that resemble those they form in cells. Self-assembly controls and amplifies reduction of 5' mRNA cap affinity of eIF4E by PML.
- Cryptic translocation of PML/RARA on 17q. A rare event in acute promyelocytic leukemia.
- PML inhibited STAT3 activity in NIH3T3, 293T, HepG2, and 32D cells. PML formed a complex with STAT3 through B-box and COOH terminal regions in vitro and in vivo, thereby inhibiting its DNA binding activity.
- In human cell lines, PML is not involved directly in the regulation of MHC class I expression.
- PML induces apoptosis through repression of the NF-kappaB survival pathway.
- Promyelocytic leukemia protein (PML) functions as a glucocorticoid receptor co-activator by sequestering Daxx to the PML oncogenic domains (PODs) to enhance its transactivation potential.
- herpes simplex virus type 1 ICP4 is recruited into foci juxtaposed to ND10 (PML) in live, infected cells
- findings strongly suggest that increased promyelocytic leukemia protein expression is associated with growth inhibition and differentiation of human neuroblastoma cells
- role of interaction in recruiting cyclin T1 to nuclear bodies
- PML regulates TopBP1 functions by association and stabilization of the protein in response to IR-induced DNA damage
- PML recruits Chk2 and p53 into the PML nuclear bodies and enhances p53/Chk2 interaction
- PML protein colocalizes and interacts with RFN36.
- PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains.
- We show here that ZIPK is present in PODs, where it colocalizes with and binds to proapoptotic protein Daxx.
- alternative splicing and role implicated in interaction with HIV-1
- Results suggest that adenovirus type 5 has evolved a unique strategy that leads to the sustained neutralization of promyelocytic leukaemia protein bodies throughout infection, thereby ensuring optimal viral proliferation.
- Leukemia-associated translocation products able to activate RAS modify PML and render cells sensitive to arsenic-induced apoptosis.
- PML-induced apoptosis by down-regulation of Survivin.
- The ectopic expression of the acute promyelocytic leukemia-specific PML/RARalpha oncoprotein in U-937 cells results in induction of TF mRNA and promoter activity
- DNA sequence variations resulting in a truncated PML protein was identified in acute promyelocytic leukemia cases that displayed retinoic acid resistance and a very poor prognosis
- PML and the PML-NB act as molecular hubs for the induction and/or reinforcement of programmed cell death through a selective and dynamic regulation of proapoptotic transcriptional events.
- Together our results suggest that PML may suppress prostate cancer cell growth by inhibiting AR transactivation and/or enhancing p53 activity.
- Data suggest that promyelocytic leukemia (PML) bodies form in nuclear compartments of high transcriptional activity, but they do not directly regulate transcription of genes in these compartments.
- PML protein expression is frequently lost in human cancers of various histologic origins, and its loss associates with tumor grade and progression in some tumor histotypes
- PML is a direct p53 target that modulates p53 effector functions.
- Results demonstrate that transcription activity associated with PML bodies is selectively repressed by the recruitment of Bach2 around PML bodies
- acute promyelocytic leukemia cell differentiation parallels transcriptional activation through PML-RARA-RXR oligomers
- interference by human Cytomegalovirus IE1 protein with both the sumoylation of PML and its repressor activity requires a physical interaction with PML that also leads to disruption of PML oncogenic domains (PODs).
- PML plays a crucial role in modulating p73 function.
- PML is a negative regulator of p38 kinase in tumor cells
- PML I could act as a mediator for acute myeloid leukemia1 and its coactivator p300/CBP to assemble into functional complexes; a specific isoform PML I forms a complex with AML1
- The 3 breakpoint cluster regions in the PML gene [Intron 6 (bcr1), exon 6 (bcr2) or intron 3 (bcr3)] were studied in 43 Mexican Mestizo APL patients. Bcr1=62.7%, bcr2=9.3% & bcr3=27.9%. Bcr1 was more prevalent than in Caucasians but similar to Asians.
- TRAILprotein is a novel downstream transcriptional target of PML.
- PML bodies control the distribution, dynamics and function of CHFR
- SUMO-1 functions to tether proteins to PML-containing nuclear bodies through post-translational modification and noncovalent protein-protein interaction
- INI1 is dispensable for retrovirus-induced cytoplasmic accumulation of PML and does not interfere with virus integration.
- PML-retinoic acid receptor alpha activities are regulated by neutrophil elastase in early myeloid cells
- CDDO-Im downregulates PML expression in acute promyleocytic leukemic cells.
- PML3 has a direct role in the control of centrosome duplication through suppression of Aurora A activation to prevent centrosome reduplication
- inhibition of monocyte differentiation all contribute to the oncogenic activity of PML-RARalpha
- IEX-1 is organized in subnuclear structures and partially co-localizes with promyelocytic leukemia protein in HeLa cells
- Isoforms of PML protein differ in their effects on ND10 organization.
- findings strengthen the relevance of the cross talk between PML and the p53 family members, imply a new tumour suppressive function of PML and unveil a possible role for PML in epidermal morphogenesis and differentiation
- loss of one copy of PU.1 through deletion, plus down-regulation of the residual allele caused by PML-RARalpha expression, synergizes to expand myeloid progenitors susceptible to transformation, increasing the penetrance of acute promyelocytic leukemia
- These results indicate that PML isoforms which are expressed in a serum-dependent manner suppress the propagation of influenza virus at an early stage of infection.
- Our work implies that the balance of promyelocytic leukemia protein and Epstein-Barr virus BZLF1 levels in cells may affect how each protein functions.
- PML-RARalpha functions by recruiting an HDAC3-MBD1 complex that contributes to the establishment and maintenance of the silenced chromatin state
- permanent transcriptional silencing is mediated by the association of PML-RAR with chromatin-modifying enzymes and by recruitment of the histone methyltransferase SUV39H1, responsible for trimethylation of lysine 9 of histone H3
- Interaction between Adenovirus type 5 E4 Orf3 and PML isoform II is necessary for nuclear domain 10 (ND10) rearrangement to occur
- PML stimulated hSUMO-1 modification in yeast, in a manner that was dependent upon PML's RING-finger domain. PML:RARalpha also stimulated hSUMO-1 conjugation in yeast.
- analysis of cytoplasmic function of mutant promyelocytic leukemia (PML) and PML-retinoic acid receptor-alpha
- frequencies of the PML-RARalpha transcripts and subtypes in a series of 32 APL patients from Northeast Brazil
- The PML-RARA fusions can be identified by molecular analyses such as reverse transcriptase-polymerase chain reaction (PCR) and fluorescence in situ hybridization (FISH).
- We show that expression of PML isoform IV leads to formation of distinct nuclear bodies enriched in components of the ubiquitin-proteasome system. These bodies recruit soluble mutant ataxin-7 and promote its degradation preventing aggregate formation
- PML contributes to a cellular antiviral repression mechanism that is countered by the activity of ICP0.
- PML functions as part of an intrinsic immune mechanism against cytomegalovirus infections.
- Our results provide evidence of how poliovirus counteracts p53 antiviral activity by regulating PML and NBs, thus leading to p53 degradation.
- The interaction of TGIF with cPML through c-Jun may negatively regulate TGF-beta signaling through controlling the localization of cPML and, consequently, the assembly of the cPML-SARA complex.
- apoptin interacts directly with the promyelocytic leukemia protein (PML) in tumor cells and accumulates in PML nuclear bodies
- In response to ATRA, PML/RARalpha is dissociated from CAK, leading to MAT1 degradation, G1 arrest, and decreased CAK phosphorylation of PML/RARalpha
- SUMO-1, PML and ZNF198 colocalize to punctate structures, shown by immunocytochemistry to be PML bodies.
- Histone deacetylase inhibitors blocked the increase of PML nuclear body number and suppressed up-regulation of PML mRNA and protein levels in several human cell lines and in normal diploid skin fibroblasts
- establish PML-mediated destabilization of Myc and the derepression of cell cycle inhibitor genes as an important regulatory mechanism that allows cell differentiation
- the role of PML cytoplasmic proteins in the regulation of p53.
- Our studies identify PML and SATB1 as a regulatory complex that governs transcription by orchestrating dynamic chromatin-loop architecture.
- The increased expression of SUMO-1 in rheumatoid arthritis (RA) synovial fibroblasts (SFs) contributes to the resistance of these cells against Fas-induced apoptosis through increased SUMOylation of nuclear PML protein.
- Results demonstrate that the gamma 1 isoform of phospholipase C associates with nuclear promyelocytic leukemia protein.
- PML may be involved in nucleolar functions of normal non-transformed or senescent cells. The absence of nucleolar PML compartment in rapidly growing tumor cells suggests that PML association with the nucleolus might be important for cell-cycle regulation
- the hormone-independent association between PML-RARalpha and coactivators contributes to its ability to regulate gene expression
- Study recapitulated the effect of PML on early steps in infection by papillomavirus, it was found that replication and transcription of transfected paillomaviral genomes were not dependent on PML.
- The type IV isoform of PML interacted with PU.1, promoted its association with p300, and then enhanced PU.1-induced transcription and granulocytic differentiation and PU.1 directly activates the transcription of the C/EBPepsilon gene.
- expression of proto-oncogene PML and HLA class I molecules were concordantly upregulated in hepatocellular carcinoma (HCC) and the expression of PML gene might be one of the mechanisms that leads to the increased expression of class I antigen in HCC
- Downregulation of the PML protein is associated with breast cancers
- Only two specific PML splice variants (PML-I and PML-IV) are efficiently targeted to the nucleolus and the abundant PML-I isoform is required for the targeting of endogenous PML proteins to this organelle.
- promyelocytic leukemia protein (PML) and hDaxx, mediate an intrinsic immune response against HCMV infection by contributing independently to the silencing of HCMV IE gene expression.
- PML/RAR gene cytogenetic abnormalities in APL
- The presence of a single PML-RARA isoform with exon 5 is associated with recurrence in acute promyelocytic leukemia
- These results would shed new insights for the molecular mechanisms of PML-RARalpha-associated leukemogenesis.
- Endogenous WRN and BLM proteins localize in nucleoli and in nuclear PML bodies defined by isoforms of the PML protein, which is a key regulator of cellular senescence.
- Binding to Pin1 results in degradation of PML in a phosphorylation-dependent manner. Degradation of PML due to Pin1 acts both to protect a breast cancer tumor cell line from hydrogen peroxide-induced death and to increase the rate of proliferation.
- In alternative lengthening of telomere cells, TRF2 inactivation/silencing triggers cellular senescence and substantial loss of telomeric DNA upon stable TRF2 knockdown.
- Overexpression of PML was associated with poor survival in gallbladder carcinomas.
- the Hes6-CBP complex in PML-NB may influence the proliferation of cells via p53-dependent and -independent pathways.
- Unexpected coupling of PML with NFAT reveals a novel mechanism underlying the diverse physiological functions of promyelocytic leukemia.
- following DNA damage, PML facilitates Thr18 phosphorylation by recruiting p53 and CK1 into PML nuclear bodies, thereby protecting p53 from inhibition by Mdm2, leading to p53 activation.
- Over-expression of PML-2KA mutant in the cytoplasm, which was generated by mutagenesis of the nuclear localization signals of PML, in MCF-7 breast cancer cells suppressed PKM2 activity and the accumulation of lactate.
- PML sequesters HDAC7 to relieve repression and up-regulate gene expression
- reorganization of the PML nuclear body by E4 ORF3 antagonizes an innate antiviral response mediated by both PML and Daxx.
- PCTA defines a new component of the TGF-beta signalling pathway that functions to facilitate Smad2 phosphorylation through controlling the accumulation of cPML into the cytoplasm, and consequently, the assembly of Smad2-receptor complex.
- These data identify a key post-translational mechanism that controls PML protein levels in cancer cells and suggest that CK2 inhibitors may be beneficial anti-cancer drugs.
- PML is involved in trichostatin A-induced apoptosis
- These results demonstrate a novel function of HDAC7 and provide a regulatory mechanism of PML sumoylation.
- PML/RARalpha fusion protein mediates the unique sensitivity to arsenic cytotoxicity in acute promyelocytic leukemia cells.
- A kinetics model for factor exchange at PML NBs and highlight potential mechanisms to regulate intranuclear trafficking of specific factors at these domains.
- PML is a novel prognostic tool for ampullary cancer patients.
- results delineate a previously unknown PML-DAXX-HAUSP molecular network controlling PTEN deubiquitinylation and trafficking, which is perturbed by oncogenic cues in human cancer
- In a series of human AMKL samples from both Down syndrome and non-Down syndrome patients, mutations were identified within KIT, FLT3, JAK2, JAK3, and MPL genes, with a higher frequency in DS than in non-DS patients.
- purified the PML complex and identified Fbxo3 (Fbx3), Skp1, and Cullin1 as novel components amd role in transcriptional regulation and leukemogenesis
- PML disruption by EBNA1 requires binding to the cellular ubiquitin specific protease, USP7 or HAUSP, but is independent of p53.
- the increase of level of survivin in tumor tissues is not the result of decrease in content of its inhibitors SMAC and PML, as their content in tumor and normal cells is the same.
- The results indicate that both sets of events mediated by ICP0, the degradation of PML and the blocking of silencing via the HDAC1/2-CoREST-REST complex, are interdependent and in large measure dependent on events in the ND10 nuclear bodies.
- DNA damage-induced PML SUMOylation and are required for the ability of PML to cooperate with HIPK2 for the induction of cell death.
- Promyelomonocytic leukemia activation is a critical early event that participates in the apoptotic demise of HIV-1-elicited syncytia.
- whereas transcriptional activation of PML-RARA is likely to control differentiation, its catabolism triggers leukemia-initiating cell eradication and long-term remission of mouse acute promyelocytic leukemia
- Acute promyelocytic leukemia with insertion of PML exon 7a and partial deletion of exon 3 of RARA is reported.
- The existence of a proapoptotic autoregulatory feedback loop between p73, YAP, and the promyelocytic leukemia (PML) tumor suppressor gene, is shown.