SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene

DeCaprio, James A.

doi:10.1016/0092-8674(88)90559-4

Cited by 1,390 publications

(690 citation statements)

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“…The CR2 domain is necessary for T antigen's ability to complex with pRb, p107 and p130 (DeCaprio et al, 1988;Dyson et al, 1989;Ewen et al, 1989). Mutants 3213 and K1 both have substitutions at amino acid 107 but 3213 has a second substitution at amino acid 108.…”

Section: Activities Dependent Upon the Amino Terminusmentioning

confidence: 99%

“…Mutants 3213 and K1 both have substitutions at amino acid 107 but 3213 has a second substitution at amino acid 108. Neither of these mutants bind pRb (Christensen and Imperiale, 1995;DeCaprio et al, 1988); however, in a baculovirus co-infection assay, both K1 and 3213 can still associate with p107 and p130 in the context of fulllength T antigen (Srinivasan et al, 1997;Pipas JM, personal communication). Taking this data together with our data, suggests that sequestration of pRb by T antigen may not be important for immortalization of rodent cells but raises the possibility that the interaction between T antigen and p130 may be critical for immortalization of rodent cells.…”

Section: Activities Dependent Upon the Amino Terminusmentioning

confidence: 99%

“…Downstream of the J domain region is the CR2 domain (amino acids 102 ± 115) with homology to adenovirus E1A proteins, human papillomavirus type 16 E7 protein and polyoma virus T antigen. The CR2 is required for binding and sequestering the retinoblastoma susceptibility protein family of pocket proteins pRb, p107 and p130 (DeCaprio et al, 1988;Moran, 1988;Ewen et al, 1989). When T antigen binds these pocket proteins, they are unable to interact with, and repress the activity of, the transcription factor E2F, so E2F-dependent transcription proceeds and the cell enters the cell cycle.…”

Section: Introductionmentioning

confidence: 99%

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Different functions are required for initiation and maintenance of immortalization of rat embryo fibroblasts by SV40 large T antigen

et al. 1999

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We have used two di erent, but complementary assays to characterize functions of SV40 T antigen that are necessary for its ability to immortalize rat embryo ®broblasts. In accordance with previous work, we found that several functions were required. These include activities that map to the p53 binding domain and the amino terminal 176 amino acids which contain the J domain as well as the CR1 and CR2 domain required for binding and sequestering the RB family of pocket proteins. Moreover, we found that even though activities dependent only upon the amino terminus were su cient for immortalization they were unable to maintain it. This suggests that immortalization by these amino terminal functions requires either additional events or immortalization of a subset of cells within the heterogeneous rat embryo ®broblast population. We further found that an activity dependent upon amino acids 17 ± 27 which remove a portion of the CR1 domain and the predicted a-1 helix of the J domain was not necessary to maintain growth but was required for direct immortalization suggesting that at least one of the functions required initially was not required to maintain the immortal state. This represents the ®rst demonstration that some of the functions required for maintenance of the immortal state di er from those required for initiation of immortalization.

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Section: Activities Dependent Upon the Amino Terminusmentioning

confidence: 99%

Section: Activities Dependent Upon the Amino Terminusmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Different functions are required for initiation and maintenance of immortalization of rat embryo fibroblasts by SV40 large T antigen

et al. 1999

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“…Co-immunoprecipitation studies in monkey cells expressing SV40 large T-antigen demonstrated that it forms a complex with pRb (DeCaprio et al, 1988). T-antigen mutants that contained structural alterations in a 10 residue, transformation-controlling domain (LXCXE domain) failed to complex with pRb indicating that transformation by SV40, at least in part, involves perturbation of the pRb protein.…”

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

confidence: 99%

“…Similarly co-immunoprecipitation studies showed that the large T-antigen of SV40 also forms a complex with pRb. Mutants of T-antigen that contained structural alterations in a 10 residue, transformation-controlling domain (LXCXE domain) failed to complex with pRb indicating that transformation by SV40, at least in part, involves perturbation of the pRb protein (DeCaprio et al, 1988). SV40 large T-antigen binds preferentially to the lower molecular weight hypophosphorylated of pRb .…”

Section: Introductionmentioning

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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A Transgenic Mouse Model for Trilateral Retinoblastoma

et al. 1990

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increase in UV light dosage without producing observable keratitis. This protective effect persists when the UV light exposure is delayed for 60 minutes after application of the chromophore. Since Parsol-MCX absorbs light in the UV-B light range, these findings are consistent with prior studies that have demonstrated UV lightinduced keratitis to be primarily due to UV-B radiation.'" We did not see any apparent toxicity immediately after application of drops containing either Parsol-1789 or Parsol-MCX or after 24 hours (Table), suggesting that these chromophores are nontoxic in the short term. Further studies are indicated to rule out possible long-term toxicity. We attempted to quantitate the reduction in UV light transmittance from topically applied chromophores in two fundamentally different waysin vitro spectrophotometric measurement of corneal transmittance and in vivo reduction of clinical UV light-induced keratitis. Since untreated normal cornea transmits little UV-B radiation, the reduction of UV light transmittance in this wavelength range by a chromophore cannot be ad

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SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene

Cited by 1,390 publications

References 64 publications

Different functions are required for initiation and maintenance of immortalization of rat embryo fibroblasts by SV40 large T antigen

Different functions are required for initiation and maintenance of immortalization of rat embryo fibroblasts by SV40 large T antigen

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

A Transgenic Mouse Model for Trilateral Retinoblastoma

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