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Vol. 13, Issue 10, 3560-3575, October 2002
Department of Pharmacology and Cancer Biology, Duke University
Medical Center, Durham, North Carolina 27710
Swe1p, the sole Wee1-family kinase in Saccharomyces
cerevisiae, is synthesized during late G1 and is then degraded
as cells proceed through the cell cycle. However, Swe1p degradation is halted by the morphogenesis checkpoint, which responds to insults that
perturb bud formation. The Swe1p stabilization promotes cell cycle
arrest through Swe1p-mediated inhibitory phosphorylation of Cdc28p
until the cells can recover from the perturbation and resume bud
formation. Swe1p degradation involves the relocalization of Swe1p from
the nucleus to the mother-bud neck, and neck targeting requires the
Swe1p-interacting protein Hsl7p. In addition, Swe1p degradation is
stimulated by its substrate, cyclin/Cdc28p, and Swe1p is thought to be
a target of the ubiquitin ligase SCFMet30 acting with the
ubiquitin-conjugating enzyme Cdc34p. The basis for regulation of Swe1p
degradation by the morphogenesis checkpoint remains unclear, and in
order to elucidate that regulation we have dissected the Swe1p
degradation pathway in more detail, yielding several novel findings.
First, we show here that Met30p (and by implication
SCFMet30) is not, in fact, required for Swe1p degradation.
Second, cyclin/Cdc28p does not influence Swe1p neck targeting, but can
directly phosphorylate Swe1p, suggesting that it acts downstream of
neck targeting in the Swe1p degradation pathway. Third, a screen for
functional but nondegradable mutants of SWE1 identified
two small regions of Swe1p that are key to its degradation. One of
these regions mediates interaction of Swe1p with Hsl7p, showing that
the Swe1p-Hsl7p interaction is critical for Swe1p neck targeting and
degradation. The other region did not appear to affect interactions
with known Swe1p regulators, suggesting that other as-yet-unknown
regulators exist.
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