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THE PHOSPHORYLATION STATE OF THE RETINOBLASTOMA (RB) PROTEIN IN G0 G1 IS DEPENDENT ON GROWTH STATUS

THOMAS, NSB; BURKE, LC; BYBEE, A; LINCH, DC; (1991) THE PHOSPHORYLATION STATE OF THE RETINOBLASTOMA (RB) PROTEIN IN G0 G1 IS DEPENDENT ON GROWTH STATUS. ONCOGENE , 6 (2) 317 - 322.

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Abstract

The product of the retinoblastoma gene (RB) is a nuclear phosphoprotein which is thought to regulate the proliferation of cells. Its phosphorylation state changes with passage through the cell cycle and it has been proposed that RB protein in its hypo-phosphorylated form prevents cells proliferating. We have investigated the phosphorylation state of the RB protein in an actively-dividing human B-lymphoblastoid cell line and after cell cycle arrest caused by alpha-Interferon (alpha-IFN). We show that the phosphorylation state of the RB protein in cells with 2N DNA content depends on whether the cells are actively cycling. Our data is compatible with the proposal that dephosphorylation of the RB protein allows cells to enter a quiescent state. This study sheds light on the molecular mechanisms which may mediate the cytostatic effects of alpha-IFN.

Type: Article
Title: THE PHOSPHORYLATION STATE OF THE RETINOBLASTOMA (RB) PROTEIN IN G0 G1 IS DEPENDENT ON GROWTH STATUS
Keywords: SUSCEPTIBILITY GENE-PRODUCT, CELL-CYCLE, OSTEO-SARCOMA, EXPRESSION, DIFFERENTIATION, PROLIFERATION, INTERFERON, SEQUENCE, MITOSIS, KINASE
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Cancer Institute
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Cancer Institute > Research Department of Haematology
URI: http://discovery.ucl.ac.uk/id/eprint/42278
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