1989
DOI: 10.1016/0092-8674(89)90840-4
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An N-Terminal transformation-governing sequence of SV40 large T antigen contributes to the binding of both p110 and a second cellular protein, p120

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Cited by 232 publications
(151 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%
See 1 more Smart Citation
“…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%
“…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%
“…As recently demonstrated, the viral antigens involved in cell transformation contain an amino acid motif (DLXCXE) that is highly conserved among the DNA tumour viruses (Moran, 1988;Figge et al, 1988). This motif has recently been shown to be essential to the transformation of rodent cells (Chen & Paucha, 1990;Barbosa et al, 1990) and to be involved in the binding of at least one tumour suppressor gene product (RB; Dyson et al, 1989;Ewen et al, 1989;Whyte et al, 1988;DeCaprio, 1988).…”
Section: Discussionmentioning
confidence: 99%
“…Whereas antibodies to pRb immunoprecipitated proteins in the range 110-114 kDa, only p110 co-immunoprecipitated with antibody to SV40 large T-antigen showing that it binds preferentially to the lower molecular weight hypophosphorylated form of pRb . The same amino-acid sequence element (LXCXE domain) of the large T-antigen protein also contributed to the formation of a complex with a second cellular protein with an apparent molecular of 120 kDa (Ewen et al, 1989). Presumably this second protein is pRb2 (see below).…”
Section: Interaction Of Sv40 Large T-antigen With Prb and Its Family mentioning
confidence: 99%