{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8(1)"],"submitter":["Tan GS"],"pubmed_abstract":["<h4>Background</h4>The execution of meiotic nuclear divisions in S. cerevisiae is regulated by protein degradation mediated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase. The correct timing of APC/C activity is essential for normal chromosome segregation. During meiosis, the APC/C is activated by the association of either Cdc20p or the meiosis-specific factor Ama1p. Both Ama1p and Cdc20p are targeted for degradation as cells exit meiosis II with Cdc20p being destroyed by APC/CAma1. In this study we investigated how Ama1p is down regulated at the completion of meiosis.<h4>Findings</h4>Here we show that Ama1p is a substrate of APC/CCdc20 but not APC/CCdh1 in meiotic cells. Cdc20p binds Ama1p in vivo and APC/CCdc20 ubiquitylates Ama1p in vitro. Ama1p ubiquitylation requ"],"journal":["Cell division"],"pagination":["9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3734102"],"repository":["biostudies-literature"],"pubmed_title":["Mutually dependent degradation of Ama1p and Cdc20p terminates APC/C ubiquitin ligase activity at the completion of meiotic development in yeast."],"pmcid":["PMC3734102"],"pubmed_authors":["Cooper KF","Lewandowski R","Mallory MJ","Tan GS","Strich R"],"additional_accession":[]},"is_claimable":false,"name":"Mutually dependent degradation of Ama1p and Cdc20p terminates APC/C ubiquitin ligase activity at the completion of meiotic development in yeast.","description":"<h4>Background</h4>The execution of meiotic nuclear divisions in S. cerevisiae is regulated by protein degradation mediated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase. The correct timing of APC/C activity is essential for normal chromosome segregation. During meiosis, the APC/C is activated by the association of either Cdc20p or the meiosis-specific factor Ama1p. Both Ama1p and Cdc20p are targeted for degradation as cells exit meiosis II with Cdc20p being destroyed by APC/CAma1. In this study we investigated how Ama1p is down regulated at the completion of meiosis.<h4>Findings</h4>Here we show that Ama1p is a substrate of APC/CCdc20 but not APC/CCdh1 in meiotic cells. Cdc20p binds Ama1p in vivo and APC/CCdc20 ubiquitylates Ama1p in vitro. Ama1p ubiquitylation requ","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Jul","modification":"2025-06-01T01:50:57.348Z","creation":"2025-06-01T01:50:57.348Z"},"accession":"S-EPMC3734102","cross_references":{"pubmed":["23816140"],"doi":["10.1186/1747-1028-8-9"]}}