T Antigens of Simian Virus 40: Molecular Chaperones for Viral Replication and Tumorigenesis

Sullivan, Christopher S.; Pipas, James M.

doi:10.1128/mmbr.66.2.179-202.2002

Cited by 224 publications

(239 citation statements)

References 275 publications

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“…The ability of the J domain to associate with domain II raises new and interesting questions about whether the J domain function of Tag may remodel protein-protein interactions that involve domain IIa and IIb, akin to those involving retinoblastoma-related proteins (32,33). Among the potential candidates for remodeling by the J domain are p53, DNA polymerase ␣-primase, RPA, and transcription factors (1)(2)(3).…”

Section: Discussionmentioning

confidence: 99%

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Partial Proteolysis of Simian Virus 40 T Antigen Reveals Intramolecular Contacts between Domains and Conformation Changes upon Hexamer Assembly

Weißhart¹,

Friedl²,

Taneja

et al. 2004

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

“…7B, dotted line) (32,33). The nuclear localization signal of Tag and a cluster of phosphorylation sites that modulate interactions between Tag hexamers to promote bidirectional DNA unwinding during viral replication are also located in the C-terminal region of domain I (1-3, 5, 6).…”

Section: Discussionmentioning

confidence: 99%

Partial Proteolysis of Simian Virus 40 T Antigen Reveals Intramolecular Contacts between Domains and Conformation Changes upon Hexamer Assembly

Weißhart¹,

Friedl²,

Taneja

et al. 2004

Journal of Biological Chemistry

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“…The N-terminal region of T-antigen is also required for this interaction and this region is known as the J-domain because of its homology to DnaJ and it confers a molecular chaperone function to T-antigen (see Sullivan and Pipas (2002) for an excellent review). Reintroducing a LXCXE domain to an N-terminally truncated T-antigen confers on cells the ability to grow to high density (Tevethia et al, 1997).…”

Section: Interaction Of Sv40 Large T-antigen With Prb and Its Family mentioning

confidence: 99%

Interaction of retinoblastoma protein family members with large T-antigen of primate polyomaviruses

White

Khalili

2006

Oncogene

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The retinoblastoma gene product pRb and other members of the Rb family of pocket proteins have a central role in the regulation of cell cycle progression. Soon after its discovery, pRb was found to interact with the transforming oncoproteins of DNA tumor viruses and this led to rapid advances in our understanding of the mechanisms of viral transformation and cell cycle progression. DNA viruses of the polyomavirus family have small, circular, double-stranded DNA genomes contained within nonenveloped icosahedral capsids and are highly tumorigenic in experimental animals. At least three types of polyomavirus infect humans: JC virus (JCV), BK virus (BKV) and Simian Vacuolating virus-40. The early region of these viruses encodes the transforming proteins large T-antigen and small t-antigen, which are involved in viral replication and also promote transformation of cells in culture and oncogenesis in vivo. Binding of T-antigen to pRb promotes the activation of the E2F family of transcription factors, which induce the expression of cellular genes required for S phase. In the context of lytic infection, this cell cycle progression is necessary for viral replication because polyomaviruses rely on S phasespecific host factors for their DNA synthesis. In the context of cellular transformation and tumorigenesis, T-antigen/pRB interaction is an indispensable event.

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“…[9][10][11][12]. The ability of T antigen to cause karyotypic instability in human cells has been found to correlate with its ability to deregulate normal mitotic checkpoints, but the exact mechanism is not known.…”

Section: Introductionmentioning

confidence: 99%

“…(reviewed in refs. [9][10][11][12]. A recent report on yeast twohybridization and immunoprecipitation techniques showed that the Bub1 gene is another targeting protein of SV40 Tag (9).…”

Section: Introductionmentioning

confidence: 99%

Bub1 Up-Regulation and Hyperphosphorylation Promote Malignant Transformation in SV40 Tag–Induced Transgenic Mouse Models

Guo

Wu²,

Chin³

et al. 2006

Molecular Cancer Research

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Rodents do not naturally develop prostate cancer. Currently, most widely used genetically engineered mouse prostate cancer models use SV40 T/tag oncogene. To understand the mechanism underlying prostate cancer development in transgenic and knock-in SV40 Tag mouse models, we did cDNA microarray analyses, comparing gene expression profiles of prostate cancer tissues from early-, late-, and advance-stage androgen-independent prostate cancers. Of the 67 genes that were up-regulated by z10-fold, 40 are known to be required for chromosome stability. In particular, the spindle checkpoint component Bub1 was persistently up-regulated from early to advanced androgen-independent prostate cancer lesions. Significantly, Bub1, which is required for accurate chromosome segregation during mitosis, has recently been reported to bind SV40 Tag. Consistent with a spindle checkpoint defect, flow cytometry experiments indicate that advanced androgen-independent prostate cancer tumors exhibit aneuploidy, along with up-regulation of levels of both Bub1 mRNA and Bub1 protein or hyperphosphorylation. Importantly, up-regulation and hyperphosphorylation of Bub1 were also observed in established human prostate cancer cell lines and in clinical studies. Furthermore, analysis of human prostate cancer lines showed impaired spindle checkpoint function and endoreduplication following exposure to spindle toxins. Small interfering RNA -mediated repression of Bub1 in the human prostate cancer line PC-3 restrained cell proliferation, an effect mimicked by inhibition of mitogen-activated protein kinase, an upstream activator of Bub1. Thus, by perturbing Bub1 function, our observations suggest a new mechanism whereby the SV40 Tag oncoprotein promotes chromosomal instability and aneuploidy in transgenic mouse prostate cancer models. Whereas the exact details of this mechanism remain unclear, our novel findings raise the possibility of exploiting Bub1 as a new therapeutic target in the treatment of prostate cancer, the most common cancer in adult men in North America. (Mol Cancer Res 2006;4(12):957 -69)

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T Antigens of Simian Virus 40: Molecular Chaperones for Viral Replication and Tumorigenesis

Cited by 224 publications

References 275 publications

Partial Proteolysis of Simian Virus 40 T Antigen Reveals Intramolecular Contacts between Domains and Conformation Changes upon Hexamer Assembly

Partial Proteolysis of Simian Virus 40 T Antigen Reveals Intramolecular Contacts between Domains and Conformation Changes upon Hexamer Assembly

Interaction of retinoblastoma protein family members with large T-antigen of primate polyomaviruses

Bub1 Up-Regulation and Hyperphosphorylation Promote Malignant Transformation in SV40 Tag–Induced Transgenic Mouse Models

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