Abstract
Exit from mitosis requires the degradation of regulatory proteins including the mitotic cyclins and securin through ubiquitination by the anaphase promoting complex (APC) bound to Cdc20 or Cdh1. Cdc20-APC is regulated through inhibition by the spindle assembly checkpoint protein MAD2. Knowledge of Cdh1-APC regulation is limited to the phosphorylation-dependent dissociation of Cdh1 from APC. We report a novel means of regulating Cdh1 by the MAD2-related gene, MAD2L2. MAD2L2 specifically binds and inhibits Cdh1-APC, paralleling the effect of MAD2 on Cdc20. We suggest that MAD2L2 and MAD2 inhibit the release of substrates from APC and propose a mechanism of inhibition.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adaptor Proteins, Signal Transducing*
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Amino Acid Sequence
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Anaphase-Promoting Complex-Cyclosome
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Animals
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Calcium-Binding Proteins
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Cdc20 Proteins
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Cell Cycle Proteins / metabolism
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Cloning, Molecular
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Fungal Proteins
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Ligases / antagonists & inhibitors
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Ligases / metabolism*
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Mad2 Proteins
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Mitosis / physiology*
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Molecular Sequence Data
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Nuclear Proteins
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Protein Binding
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
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Ubiquitin-Protein Ligase Complexes*
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Ubiquitin-Protein Ligases
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Xenopus
Substances
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Adaptor Proteins, Signal Transducing
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CDC20 protein, S cerevisiae
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Calcium-Binding Proteins
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Carrier Proteins
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Cdc20 Proteins
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Cell Cycle Proteins
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Fungal Proteins
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MAD2 protein, S cerevisiae
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MAD2L2 protein, Xenopus
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Mad2 Proteins
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Nuclear Proteins
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Saccharomyces cerevisiae Proteins
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Ubiquitin-Protein Ligase Complexes
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Anaphase-Promoting Complex-Cyclosome
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Ubiquitin-Protein Ligases
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Ligases