{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hinshaw SM"],"funding":["University of California San Diego","Howard Hughes Medical Institute","University of California","National Institutes of Health","Helen Hay Whitney Foundation","NIH HHS","NIGMS NIH HHS"],"pagination":["688-696.e6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9992315"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["33(4)"],"pubmed_abstract":["Kinetochores control eukaryotic chromosome segregation by connecting chromosomal centromeres to spindle microtubules. Duplication of centromeric DNA necessitates kinetochore disassembly and subsequent reassembly on nascent sisters. To search for a regulatory mechanism that controls the earliest steps of this process, we studied Mif2/CENP-C, an essential basal component of the kinetochore. We found that phosphorylation of a central region of Mif2 (Mif2-PEST) enhances inner kinetochore assembly. Eliminating Mif2-PEST phosphorylation sites progressively impairs cellular fitness. The most severe Mif2-PEST mutations are lethal in cells lacking otherwise non-essential inner kinetochore factors. These data show that multi-site phosphorylation of Mif2/CENP-C controls inner kinetochore assembly."],"journal":["Current biology : CB"],"pubmed_title":["Multi-site phosphorylation of yeast Mif2/CENP-C promotes inner kinetochore assembly."],"pmcid":["PMC9992315"],"funding_grant_id":["S10 OD023498","OD023498","R01 GM116897","GM116897"],"pubmed_authors":["Cai J","Quan Y","Zhou AL","Zhou H","Hinshaw SM"],"additional_accession":[]},"is_claimable":false,"name":"Multi-site phosphorylation of yeast Mif2/CENP-C promotes inner kinetochore assembly.","description":"Kinetochores control eukaryotic chromosome segregation by connecting chromosomal centromeres to spindle microtubules. Duplication of centromeric DNA necessitates kinetochore disassembly and subsequent reassembly on nascent sisters. To search for a regulatory mechanism that controls the earliest steps of this process, we studied Mif2/CENP-C, an essential basal component of the kinetochore. We found that phosphorylation of a central region of Mif2 (Mif2-PEST) enhances inner kinetochore assembly. Eliminating Mif2-PEST phosphorylation sites progressively impairs cellular fitness. The most severe Mif2-PEST mutations are lethal in cells lacking otherwise non-essential inner kinetochore factors. These data show that multi-site phosphorylation of Mif2/CENP-C controls inner kinetochore assembly.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2025-04-03T23:49:49.667Z","creation":"2025-04-03T23:49:49.667Z"},"accession":"S-EPMC9992315","cross_references":{"pubmed":["36736323"],"doi":["10.1016/j.cub.2023.01.012"]}}