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J Biol Chem, Vol. 273, Issue 37, 23659-23667, September 11, 1998
-Interferon
From the Department of Haematology, University College London
Medical School, 98 Chenies Mews, London
WC1E 6HX, United Kingdom.
We have determined how the phosphorylation of the
retinoblastoma family (pRb, p107, and p130) is governed in individual
cell cycle phases of Daudi B-cells during cell cycle exit triggered by
-interferon (-IFN). -IFN causes dephosphorylation of pRb and
loss of p130 phosphorylated Form 3. However, the change in p130
phosphorylation in response to -IFN occurs before dephosphorylation of pRb is complete because loss of p130 Form 3 occurs throughout the
cell cycle prior to complete arrest in G1, whereas pRb is dephosphorylated only in G1. In contrast, p107 is
dephosphorylated and is then depleted from cells as they exit the cell
cycle. p130, predominantly in Form 1, and hypophosphorylated pRb bind
an E2F DNA binding site; p130 complexes E2F-4, whereas pRb binds both E2F-4 and E2F-1. The phosphorylated forms of E2F-4 that bind to the E2F
DNA site are different from hyperphosphorylated E2F-4, which
predominates in primary hemopoietic cells in G0. We
conclude that although cell cycle arrest induced by -IFN may be
mediated in part by formation of a complex containing p130 and E2F-4,
-IFN does not induce hyperphosphorylation of E2F-4, which
characterizes primary hemopoietic cells in G0.
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