Intranuclear Redistribution of SV40T, p53, and PML in a Conditionally SV40T-Immortalized Cell Line

Jiang, Wei‐Qin; Szekeres, L.; Klein, George; Ringertz, Nils R.

doi:10.1006/excr.1996.0374

Cited by 20 publications

(13 citation statements)

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“…This proposal would partly explain why the HCMV IE2 protein precisely colocalizes with ND10 in transfected cells but forms juxtaposed foci during infection (23); in transfected cells, IE2 may be aberrantly located because viral genomes are absent, so the protein is unable to assemble into the macromolecular complexes characteristic of a viral infection. We note that simian virus 40 (SV40) large T antigen, a transcriptional regulator with many functional similarities to IE2 and ICP4, also forms foci adjacent to ND10 (7,14,25), as do model SV40 genomes (43). Therefore, the related but different localizations of ICP0 and ICP4 may reflect a situation that is common to many different viral infections.…”

Section: Discussionmentioning

confidence: 93%

Recruitment of Herpes Simplex Virus Type 1 Transcriptional Regulatory Protein ICP4 into Foci Juxtaposed to ND10 in Live, Infected Cells

Everett¹,

Sourvinos²,

Orr³

2003

J Virol

123

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At the early stages of herpes simplex virus type 1 (HSV-1) infection, parental viral genomes have a tendency to become juxtaposed to cellular nuclear structures known as PML (promyelocytic leukemia) nuclear bodies or ND10, while the immediate-early (IE) protein ICP0 precisely colocalizes with these structures. Previous indirect-immunofluorescence studies observed that the HSV-1 transcriptional regulator ICP4 has a mainly diffuse nuclear distribution early in infection and is later recruited into viral replication compartments. We have constructed HSV-1 variants expressing ICP4 and ICP0 linked to ECFP and EYFP, respectively, both singly and in combination. Coupled with an efficient method of expressing autofluorescent PML in ND10, we have studied the dynamics of ICP0, ICP4, and ND10 in live, infected cells. The greater sensitivity and lower background signals in live cells revealed that early in infection, ICP4 forms discrete foci, some of which are juxtaposed to ND10, while ICP0 was found to colocalize precisely with PML. As expected from these results, using a double-labeled virus, we observed that foci of ICP0 and ICP4 were also juxtaposed but not colocalized early in infection. Some of the ICP4 foci must have contained parental viral genomes, because they developed into replication compartments. We propose that a proportion of the ND10-associated ICP4 foci represent ICP4 molecules being recruited onto parental viral genomes, a process likely to be a critical step early in lytic infection. These results may be analogous to the localization of IE1 and IE2 during human cytomegalovirus infection, suggesting a principle common to the alpha-and betaherpesviruses.

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Section: Discussionmentioning

confidence: 93%

Recruitment of Herpes Simplex Virus Type 1 Transcriptional Regulatory Protein ICP4 into Foci Juxtaposed to ND10 in Live, Infected Cells

Everett¹,

Sourvinos²,

Orr³

2003

J Virol

123

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“…4B below). In Idh4 cells, which conditionally express the SV40T oncogene, loss of SV40T expression induces senescence and changes in the morphology of PML bodies (Jiang et al, 1996;Jiang and Ringertz, 1997). In oncogene-deprived senescent Idh4 cells, as above in WI-38 cells, PML, Daxx, Sp100 and SUMO usually labelled the outer shell, whereas fibrillarin, B23 and UBF stained the inner part of the structure (Fig.…”

Section: (Data Not Shown)mentioning

confidence: 99%

“…Idh4 (a gift from Woodring E. Wright, UT Southwestern Medical Centre, Dallas, TX) were cultured in DMEM with 10% charcoil-depleted serum (ironsupplemented bovine serum; Perbio, Erembodegen, Belgium) and 5 M dexamethasone. Senescence was induced by depletion of dexamethasone, as previously described (Jiang et al, 1996;Jiang and Ringertz, 1997). Pml -/-MEFs were obtained from 13-to 14-day mouse embryos.…”

Section: Cell-lines Transfection and Treatmentmentioning

confidence: 99%

A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells

Condemine

Takahashi

Bras

et al. 2007

Journal of Cell Science

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The promyelocytic leukemia (PML) tumour suppressor is the organiser of PML nuclear bodies, which are domains the precise functions of which are still disputed. We show that upon several types of stress, endogenous PML proteins form nucleolar caps and eventually engulf nucleolar components. 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. We identified a nucleolar targeting domain within the evolutionarily conserved C-terminus of PML-I. This domain contains a predicted exonuclease III fold essential for the targeting of the PML-I C-terminus to nucleolar fibrillar centres. Furthermore, spontaneous or oncogene retrieval-induced senescence is associated with the formation of very large PML nuclear bodies that initially contain nucleolar components. Later, poly-ubiquitin conjugates are found on the outer shell or within most of these senescence-associated PML bodies. Thus, unexpectedly, the scarcely studied PML-I isoform links PML bodies, nucleolus, senescence and proteolysis.

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“…SV40 large T antigen activates viral DNA replication by binding to the viral replication origin and in part localizes in foci juxtaposed to PML NBs in transfected, infected and transformed cells (Carvalho et al, 1995;Doucas et al, 1996;Jiang et al, 1996). SV40 DNA replication also occurs in similar PML body-associated foci , and the localization of SV40 genomes to the periphery of ND10 requires both SV40 large T antigen and an intact SV40 origin of DNA replication (Tang et al, 2000).…”

Section: Papovavirusesmentioning

confidence: 99%

DNA viruses and viral proteins that interact with PML nuclear bodies

Everett¹

2001

Oncogene

230

238

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Connections between PML nuclear bodies (PML NBs) and DNA virus replication have been investigated from the earliest days of the molecular characterization of PML and associated proteins. It appears to be a general feature of nuclear-replicating DNA viruses that their parental genomes preferentially become associated with PML NBs, and that their initial sites of transcription and development of DNA replication centres are frequently juxtaposed to these domains or their remnants. In addition, regulatory proteins encoded by several DNA viruses associate with and sometimes cause catastrophic changes to PML NBs by a variety of mechanisms. These events can be correlated with the eciency of viral infection and the functions of viral regulatory proteins, but the underlying molecular connections between PML NB function and viral infection remain poorly understood. This article reviews the latest developments in the interactions between PML NBs and herpesviruses, adenoviruses and papovaviruses. Oncogene (2001) 20, 7266 ± 7273.

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Intranuclear Redistribution of SV40T, p53, and PML in a Conditionally SV40T-Immortalized Cell Line

Cited by 20 publications

References 0 publications

Recruitment of Herpes Simplex Virus Type 1 Transcriptional Regulatory Protein ICP4 into Foci Juxtaposed to ND10 in Live, Infected Cells

Recruitment of Herpes Simplex Virus Type 1 Transcriptional Regulatory Protein ICP4 into Foci Juxtaposed to ND10 in Live, Infected Cells

A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells

DNA viruses and viral proteins that interact with PML nuclear bodies

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