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Vol. 9, Issue 7, 1817-1831, July 1998
Research Institute of Molecular Pathology, A-1030 Vienna, Austria
The initiation of anaphase and exit from mitosis depend on the
anaphase-promoting complex (APC), which mediates the
ubiquitin-dependent proteolysis of anaphase-inhibiting proteins and
mitotic cyclins. We have analyzed whether protein phosphatases are
required for mitotic APC activation. In Xenopus egg
extracts APC activation occurs normally in the presence of protein
phosphatase 1 inhibitors, suggesting that the anaphase defects caused
by protein phosphatase 1 mutation in several organisms are not due to a
failure to activate the APC. Contrary to this, the initiation of
mitotic cyclin B proteolysis is prevented by inhibitors of protein
phosphatase 2A such as okadaic acid. Okadaic acid induces an activity
that inhibits cyclin B ubiquitination. We refer to this activity as inhibitor of mitotic proteolysis because it also prevents the degradation of other APC substrates. A similar activity exists in
extracts of Xenopus eggs that are arrested at the second
meiotic metaphase by the cytostatic factor activity of the protein
kinase mos. In Xenopus eggs, the initiation of anaphase
II may therefore be prevented by an inhibitor of APC-dependent
ubiquitination.
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