Abstract
Anaphase-promoting complex (APC), a ubiquitin ligase, controls both sister chromatid separation and mitotic exit. The APC is activated in mitosis and G1 by CDC20 and CDH1, and inhibited by the checkpoint protein MAD2, a specific inhibitor of CDC20. We show here that a MAD2 homolog MAD2B also inhibits APC. In contrast to MAD2, MAD2B inhibits both CDH1-APC and CDC20-APC. This inhibition is targeted to CDH1 and CDC20, but not directly to APC. Unlike MAD2, whose interaction with MAD1 is required for mitotic checkpoint control, MAD2B does not interact with MAD1, suggesting that MAD2B may relay a different cellular signal to APC.
MeSH Terms
Anaphase-Promoting Complex-Cyclosome
Animals
Cdc20 Proteins
Cell Cycle Proteins/metabolism
Chromatids/physiology
Cloning, Molecular
Cyclin B/metabolism
Humans
Ligases/antagonists & inhibitors
Mad2 Proteins
Mitosis/physiology
Nuclear Proteins
Phosphoproteins/metabolism
Proteins/genetics,metabolism
Repressor Proteins/metabolism
Saccharomyces cerevisiae Proteins
Subcellular Fractions/metabolism
Ubiquitin-Protein Ligase Complexes
Ubiquitin-Protein Ligases
Xenopus
Chemicals
CDC20 protein, S cerevisiae
Cdc20 Proteins
Cell Cycle Proteins
Cyclin B
MAD1 protein, S cerevisiae
MAD1L1 protein, human
MAD2L2 protein, human
Mad2 Proteins
Nuclear Proteins
Phosphoproteins
Proteins
Repressor Proteins
Saccharomyces cerevisiae Proteins
Ubiquitin-Protein Ligase Complexes
Anaphase-Promoting Complex-Cyclosome
Ubiquitin-Protein Ligases
Ligases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Chen J
Department of Biological Sciences, Stanford University, Stanford, California 94305-5020, USA.
Fang G
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