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http://purl.uniprot.org/citations/37067150http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37067150http://www.w3.org/2000/01/rdf-schema#comment"Phosphorylation is a key post-translational modification that is utilised in many biological processes for the rapid and reversible regulation of protein localisation and activity. Polo-like kinase 1 (PLK-1) is essential for both mitotic and meiotic cell divisions, with key functions being conserved in eukaryotes. The roles and regulation of PLK-1 during mitosis have been well characterised. However, the discrete roles and regulation of PLK-1 during meiosis have remained obscure. Here, we used Caenorhabditis elegans oocytes to show that PLK-1 plays distinct roles in meiotic spindle assembly and/or stability, chromosome alignment and segregation, and polar body extrusion during meiosis I. Furthermore, by a combination of live imaging and biochemical analysis we identified the chromosomal recruitment mechanisms of PLK-1 during C. elegans oocyte meiosis. The spindle assembly checkpoint kinase BUB-1 directly recruits PLK-1 to the kinetochore and midbivalent while the chromosome arm population of PLK-1 depends on a direct interaction with the centromeric-associated protein CENP-CHCP-4. We found that perturbing both BUB-1 and CENP-CHCP-4 recruitment of PLK-1 leads to severe meiotic defects, resulting in highly aneuploid oocytes. Overall, our results shed light on the roles played by PLK-1 during oocyte meiosis and provide a mechanistic understanding of PLK-1 targeting to meiotic chromosomes."xsd:string
http://purl.uniprot.org/citations/37067150http://purl.org/dc/terms/identifier"doi:10.7554/elife.84057"xsd:string
http://purl.uniprot.org/citations/37067150http://purl.uniprot.org/core/author"Pelisch F."xsd:string
http://purl.uniprot.org/citations/37067150http://purl.uniprot.org/core/author"Houston J."xsd:string
http://purl.uniprot.org/citations/37067150http://purl.uniprot.org/core/author"Cheerambathur D.K."xsd:string
http://purl.uniprot.org/citations/37067150http://purl.uniprot.org/core/author"Soubigou F."xsd:string
http://purl.uniprot.org/citations/37067150http://purl.uniprot.org/core/author"Bel Borja L."xsd:string
http://purl.uniprot.org/citations/37067150http://purl.uniprot.org/core/author"Taylor S.J.P."xsd:string
http://purl.uniprot.org/citations/37067150http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37067150http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/37067150http://purl.uniprot.org/core/pages"e84057"xsd:string
http://purl.uniprot.org/citations/37067150http://purl.uniprot.org/core/title"BUB-1 and CENP-C recruit PLK-1 to control chromosome alignment and segregation during meiosis I in C. elegans oocytes."xsd:string
http://purl.uniprot.org/citations/37067150http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/37067150http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/37067150
http://purl.uniprot.org/citations/37067150http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/37067150
http://purl.uniprot.org/uniprot/#_P34331-mappedCitation-37067150http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/37067150
http://purl.uniprot.org/uniprot/#_Q21776-mappedCitation-37067150http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/37067150
http://purl.uniprot.org/uniprot/P34331http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/37067150
http://purl.uniprot.org/uniprot/Q21776http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/37067150