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J Biol Chem, Vol. 274, Issue 17, 12009-12016, April 23, 1999
From the The pocket protein-E2F complexes are convergence
points for cell cycle signaling. In the present report, we identified
and monitored the pocket protein-E2F complexes in human primary
B-lymphocytes after activation by phorbol 12-myristate 13-acetate.
Consistent with previous data from human and mouse fibroblasts and
T-lymphocytes, E2F4 and DP1 form the predominant E2F heterodimers both
in G0 and G1 phases of the human
B-lymphocyte cell cycle, whereas E2F1 and -3 are first detected in late
G1, and their expression levels increase towards S phase.
Intriguingly, the major E2F complex that we detected in quiescent human
B-lymphocytes is consisted of pRB, E2F4, and DP1. Though the levels of
DP1 and -2 increase when cells progress from G0 to S, the
proportion of DP1 to DP2 remains relatively constant during the cell
cycle. We also observed an increase in electrophoretic mobility of the
predominant E2F components, DP1 and E2F4, as B-lymphocytes progressed
from G0 into early G1. This increase in
mobility was attributable to dephosphorylation, as
Modulation of E2F Complexes during G0 to S Phase
Transition in Human Primary B-lymphocytes
,
Ludwig Institute for Cancer Research and
Section of Virology and Cell Biology,
phosphatase
treatment could convert the slower migrating forms into the
corresponding faster mobility forms. We further demonstrated that this
change in phosphorylation status correlates with a decrease in DNA
binding activity. This modulation of DNA binding activity mediated
through the dephosphorylation of DP1 and E2F4 could help to explain the
lack of in vivo DNA footprinting in late G1 and
S phases of gene promoters negatively regulated through E2F sites and
suggests a novel mechanism for controlling E2F transcriptional activity
during the transition from quiescence to proliferation.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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