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Vol. 12, Issue 11, 3402-3416, November 2001
Department of Biology, Johns Hopkins University, Baltimore,
Maryland 21218
Saccharomyces cerevisiae Cin8p belongs to the BimC
family of kinesin-related motor proteins that are essential for spindle assembly. Cin8p levels were found to oscillate in the cell cycle due in
part to a high rate of degradation imposed from the end of mitosis
through the G1 phase. Cin8p degradation required the anaphase-promoting
complex ubiquitin ligase and its late mitosis regulator Cdh1p but not
the early mitosis regulator Cdc20p. Cin8p lacks a functional
destruction box sequence that is found in the majority of
anaphase-promoting complex substrates. We carried out an extensive
mutagenesis study to define the cis-acting sequence required for Cin8p degradation in vivo. The C terminus of Cin8p contains two elements required for its degradation: 1) a bipartite destruction sequence composed of a KEN-box plus essential residues within the downstream 22 amino acids and 2) a nuclear localization signal. The bipartite destruction sequence appears in other BimC kinesins as well. Expression of nondegradable Cin8p showed very mild
phenotypic effects, with an increase in the fraction of mitotic cells
with broken spindles.
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