{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fischer ES"],"funding":["Cancer Research UK","The Francis Crick Institute","Medical Research Council","Wellcome Trust"],"pagination":["6381"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9605988"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["In response to improper kinetochore-microtubule attachments in mitosis, the spindle assembly checkpoint (SAC) assembles the mitotic checkpoint complex (MCC) to inhibit the anaphase-promoting complex/cyclosome, thereby delaying entry into anaphase. The MCC comprises Mad2:Cdc20:BubR1:Bub3. Its assembly is catalysed by unattached kinetochores on a Mad1:Mad2 platform. Mad1-bound closed-Mad2 (C-Mad2) recruits open-Mad2 (O-Mad2) through self-dimerization. This interaction, combined with Mps1 kinase-mediated phosphorylation of Bub1 and Mad1, accelerates MCC assembly, in a process that requires O-Mad2 to C-Mad2 conversion and concomitant binding of Cdc20. How Mad1 phosphorylation catalyses MCC assembly is poorly understood. Here, we characterized Mps1 phosphorylation of Mad1 and obtained structura"],"journal":["Nature communications"],"pubmed_title":["Juxtaposition of Bub1 and Cdc20 on phosphorylated Mad1 during catalytic mitotic checkpoint complex assembly."],"pmcid":["PMC9605988"],"funding_grant_id":["24307","10029","MC_UP_1201/6","FC001029","DRCRPG-Jun22\\100004","C576/A14109","CC1078","MC_U105184326","14109"],"pubmed_authors":["Maslen SL","Heck AJR","Hevler JF","Freund SMV","McLaughlin SH","Fischer ES","Barford D","Yu CWH"],"additional_accession":[]},"is_claimable":false,"name":"Juxtaposition of Bub1 and Cdc20 on phosphorylated Mad1 during catalytic mitotic checkpoint complex assembly.","description":"In response to improper kinetochore-microtubule attachments in mitosis, the spindle assembly checkpoint (SAC) assembles the mitotic checkpoint complex (MCC) to inhibit the anaphase-promoting complex/cyclosome, thereby delaying entry into anaphase. The MCC comprises Mad2:Cdc20:BubR1:Bub3. Its assembly is catalysed by unattached kinetochores on a Mad1:Mad2 platform. Mad1-bound closed-Mad2 (C-Mad2) recruits open-Mad2 (O-Mad2) through self-dimerization. This interaction, combined with Mps1 kinase-mediated phosphorylation of Bub1 and Mad1, accelerates MCC assembly, in a process that requires O-Mad2 to C-Mad2 conversion and concomitant binding of Cdc20. How Mad1 phosphorylation catalyses MCC assembly is poorly understood. Here, we characterized Mps1 phosphorylation of Mad1 and obtained structura","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2026-05-28T00:37:24.057Z","creation":"2025-04-06T21:03:55.825Z"},"accession":"S-EPMC9605988","cross_references":{"pubmed":["36289199"],"doi":["10.1038/s41467-022-34058-2"]}}