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A 20s complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B

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King, Randall W, Peters, Jan-Michael, Tugendreich, Stuart, Rolfe, Mark, Hieter, Philip, Kirschner, Marc W·1995·Cell

Abstract

Cyclin B is degraded at the onset of anaphase by a ubiquitin-dependent proteolytic system. We have fractionated mitotic Xenopus egg extracts to identify components required for this process. We find that UBC4 and at least one other ubiquitin-conjugating enzyme can support cyclin B ubiquitination. The mitotic specificity of cyclin ubiquitination is determined by a 20S complex that contains homologs of budding yeast CDC16 and CDC27. Because these proteins are required for anaphase in yeast and mammalian cells, we refer to this complex as the anaphase-promoting complex (APC). CDC27 antibodies deplete APC activity, while immunopurified CDC27 complexes are sufficient to complement either interphase extracts or a mixture of recombinant UBC4 and the ubiquitin-activating enzyme E1. These results suggest that APC functions as a regulated ubiquitin-protein ligase that targets cyclin B for destruction in mitosis.

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Metadata

Authors
King, R. W., Peters, J.-M., Tugendreich, S., Rolfe, M., Hieter, P., & Kirschner, M. W.
Venue
Cell
Publisher
Elsevier BV
Published
1995-04
Volume
81
Issue
2
Pages
279-288
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2005717642
Cited by
955
References
0
FWCI
31.62
Type
journal article
Language
en
Open access
hybrid

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King, R. W., Peters, J.-M., Tugendreich, S., Rolfe, M., Hieter, P., & Kirschner, M. W. (1995). A 20s complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B. Cell. https://doi.org/10.1016/0092-8674(95)90338-0

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