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Vol. 13, No. 18, pp. 2375-2387, September 15, 1999
1 Division of Basic Sciences, Cyclin E is an unstable protein that is degraded in a ubiquitin- and
proteasome- dependent pathway. Two factors stimulate cyclin E
ubiquitination in vivo: when it is free of its CDK partner, and when it
is phosphorylated on threonine 380. We pursued the first of these
pathways by using a two-hybrid screen to identify proteins that could
bind only to free cyclin E. This resulted in the isolation of human
Cul-3, a member of the cullin family of E3 ubiquitin-protein ligases.
We found that Cul-3 was bound to cyclin E but not to cyclin E-Cdk2
complexes in mammalian cells, and that overexpression of Cul-3
increased ubiquitination of cyclin E but not other cyclins. Conversely,
deletion of the Cul-3 gene in mice caused increased
accumulation of cyclin E protein, and had cell-type-specific effects on
S-phase regulation. In the extraembryonic ectoderm, in which cells
undergo a standard mitotic cycle, there was a greatly increased number
of cells in S phase. In the trophectoderm, in which cells go through
endocycles, there was a block to entry into S phase. The SCF pathway,
which targets cyclins for ubiquitination on the basis of their
phosphorylation state, and the Cul-3 pathway, which selects cyclin E
for ubiquitination on the basis of its assembly into CDK complexes, may
be complementary ways to control cyclin abundance.
[Key Words:
Cullins; ubiquitin degradation; cyclins; S phase]
GENES & DEVELOPMENT 13:2375-2387 © 1999 by Cold Spring Harbor Laboratory Press ISSN 0890-9369/99 $5.00
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