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Retinoblastoma protein

The retinoblastoma protein was identified originally through studies of an inherited form of eye cancer in children, known as retinoblastoma. The loss of both copies of the Rb gene leads to excessive cell proliferation in the mature retina. This suggested that... [Pg.1070]

Hinds, P. H., Mittnacht, S., Dulic, V., Arnold, A., Reed, S. I., and Weilberg, R. A. (1992). Regulation of the retinoblastoma protein functions by ectopic expression of human cyclins. Cell 70 993-1006. [Pg.42]

Gu, W., Schneider, J.W., Condorelli, G., Kaushal, S., Mahdavi, V. and Nadal-Ginard, B. (1993) Interaction of myogenic factors and the retinoblastoma protein mediates muscle cell commitment and differentiation. Cell 72, 309-324. [Pg.142]

Shi SR, Cote RJ, Yang C, et al. Development of an optimal protocol for antigen retrieval a test battery approach exemplified with reference to the staining of retinoblastoma protein (pRB) in formalin-fixed paraffin sections. J. Pathol. 1996 179 347-352. [Pg.21]

Puga, A., et. al., Aromatic hydrocarbon receptor interaction with the retinoblastoma protein potentiates repression of E2F-dependent transcription and cell cycle arrest, J. Biol. Chem., 275, 2943, 2000. [Pg.251]

Figure 26.1 Immortalization of human cells Cells enter replicative senescence at mortality stage 1 (Ml Hayflick limit) after about 60 population doublings (PD). The protein p 16 accumulates in senescent cells. The simian virus 40 (SV40) large T antigen as well as the human papilloma virus (HPV) type 16-E6 and E7 proteins sequester the retinoblastoma protein (Rb) and/or p53 constitutively releases the transcription factor E2F. E2F induces expression proteins required for progression through Gl/S transition, thus the cells escape cell cycle arrest. At mortality stage 2 (M2), transformed cells must overcome senescence and crisis before they are immortalized. This is likely to involve the activation of telomerase either by the introduction of hTERT cDNA or by a genetic change that activates telomerase. Figure 26.1 Immortalization of human cells Cells enter replicative senescence at mortality stage 1 (Ml Hayflick limit) after about 60 population doublings (PD). The protein p 16 accumulates in senescent cells. The simian virus 40 (SV40) large T antigen as well as the human papilloma virus (HPV) type 16-E6 and E7 proteins sequester the retinoblastoma protein (Rb) and/or p53 constitutively releases the transcription factor E2F. E2F induces expression proteins required for progression through Gl/S transition, thus the cells escape cell cycle arrest. At mortality stage 2 (M2), transformed cells must overcome senescence and crisis before they are immortalized. This is likely to involve the activation of telomerase either by the introduction of hTERT cDNA or by a genetic change that activates telomerase.
Acetylation levels of histone and non-histone proteins are regulated upon DNA damage. Retinoblastoma protein pRb controls Gl-S phase transition and phosphorylation of pRb regulates it function. DNA damage induced acetylation of pRb near the phosphorylation sites prevents it phosphorylation and keep pRb in active form thereby leading to growth repression. DNA damage dependant association... [Pg.203]

RIZl was originally isolated as a molecule associating with the retinoblastoma protein, Rb (Buyse et al, 1995). RIZl is classified as a member of the PR-domain family (PRDM-2) (the PR-domain family is now a sub-family of the SET-domain family proteins). It exerts H3K9 methyltransferase activity (Derunes et al, 2005). [Pg.339]

Buyse IM, Shao G, Huang S (1995) The retinoblastoma protein binds to RIZ, a zinc-finger protein that shares an epitope with the adenovirus ElA protein. Proc Natl Acad Sci USA 92 4467-4471... [Pg.346]

Figure 21.16 k diagram of the mechanism by which retinoblastoma protein (Rb) regulates transcription factor activity. The rb protein binds to the transcription factor, which forms a complex in which the transcription factor for three genes is inactive. Phosphorylation of Rb by a cell division cycle kinase results in dissociation of transcription factor from the complex and hence activation. [Pg.495]

Fig. 4. Domain structure of mammalian DNA methyltransferases. (a) The domain structure of the known DNA methyltransferases, depicting the conserved catalytic domain (dark box) and other identified domains. Conserved aminoacid motifs in the catalytic domain are shown in lighter shade of gray. (b) Schematic representation of the reported protein-protein interactions of Dnmtl with a number of regulatory proteins interactions that modulate Dnmtl methyitransferase activity (darker rectangles) or mediate methylation-independent transcriptional repression mechanisms (lighter rectangles). When Dnmtl represses transcription through its enzymatic activity, it has been described to interact with some proteins PCNA [37] and an oncogenic transcription factor PML-RAR [25]. Note that in the case of the PML-RAR transcription factor, histone deacetylase 1 (HDACl) is also bound to the complex. When Dnmtl represses transcription via methylation-independent pathways, it binds to HDACs either directly [34] or indirectly through other proteins the corepressor DMAPl [33], the retinoblastoma protein, and a gene-specific transcription factor [31]. Fig. 4. Domain structure of mammalian DNA methyltransferases. (a) The domain structure of the known DNA methyltransferases, depicting the conserved catalytic domain (dark box) and other identified domains. Conserved aminoacid motifs in the catalytic domain are shown in lighter shade of gray. (b) Schematic representation of the reported protein-protein interactions of Dnmtl with a number of regulatory proteins interactions that modulate Dnmtl methyitransferase activity (darker rectangles) or mediate methylation-independent transcriptional repression mechanisms (lighter rectangles). When Dnmtl represses transcription through its enzymatic activity, it has been described to interact with some proteins PCNA [37] and an oncogenic transcription factor PML-RAR [25]. Note that in the case of the PML-RAR transcription factor, histone deacetylase 1 (HDACl) is also bound to the complex. When Dnmtl represses transcription via methylation-independent pathways, it binds to HDACs either directly [34] or indirectly through other proteins the corepressor DMAPl [33], the retinoblastoma protein, and a gene-specific transcription factor [31].
Fig. 13.13. Domain structure of the retinoblastoma protein pRb. The phosphorylation sites (P) of pRb and the localization of the sequence sections necessary for interaction with viral oncoproteins and with the transcription factor E2F are shown. In addition, an oligomerization domain and a DNA binding domain can be identified. Fig. 13.13. Domain structure of the retinoblastoma protein pRb. The phosphorylation sites (P) of pRb and the localization of the sequence sections necessary for interaction with viral oncoproteins and with the transcription factor E2F are shown. In addition, an oligomerization domain and a DNA binding domain can be identified.
Brehm, A., Miska, E.A., McCance, D.J., Reid, J.L., Bannister, A.J. and Kouzarides, T. Retinoblastoma protein recruits histone deacetylase to repress transcription (1998) Nature 391, 597-601... [Pg.417]

Magnaghi-Jauhn, L., Groisman, R., Naguibneva, I., Robin, P, Lorain, S., Le Villain,. IP, Troalen, E, Trouche, D., Harel-Bellan, A. Retinoblastoma protein represses transcription by recruiting a histone deacetylase (1998) Nature 391, 601-605... [Pg.418]

Weinberg, R.A. The retinoblastoma protein and cell cycle control (1995) Cell 81, 323-330... [Pg.419]


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