Ubiquitin-mediated proteolysis of cell cycle regulators is a crucial proces
s during the cell cycle. The anaphase-promoting complex (APC) is a large, m
ultiprotein complex whose ES-ubiquitin ligase activity is required for the
ubiquitination of mitotic cyclins and other regulatory proteins that are ta
rgeted for destruction during cell division. The recent identification of n
ew APC subunits and regulatory proteins has begun to reveal some of the int
ricate mechanisms that govern APC regulation. One mechanism is the use of s
pecificity factors to impose temporal control over substrate degradation. A
second mechanism is the APC-mediated proteolysis of specific APC regulator
s. Finally, components of both the APC and the SCF E3 ubiquitin-ligase comp
lex contain several conserved sequence motifs, including WD-40 repeats and
cullin homology domains, which suggest that both complexes may use a simila
r mechanism for substrate ubiquitination.