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Spatiotemporal regulation of Aurora B recruitment ensures release of cohesion during C. elegans oocyte meiosis

N. Ferrandiz,C. Barroso,Oana Telecan,Nan Shao,Hyun-Min Kim,S. Testori,P. Faull,P. Cutillas,A. Snijders,M. Colaiácovo,E. Martinez-Perez

Published 2018 in Nature Communications

ABSTRACT

The formation of haploid gametes from diploid germ cells requires the regulated two-step release of sister chromatid cohesion (SCC) during the meiotic divisions. Here, we show that phosphorylation of cohesin subunit REC-8 by Aurora B promotes SCC release at anaphase I onset in C. elegans oocytes. Aurora B loading to chromatin displaying Haspin-mediated H3 T3 phosphorylation induces spatially restricted REC-8 phosphorylation, preventing full SCC release during anaphase I. H3 T3 phosphorylation is locally antagonized by protein phosphatase 1, which is recruited to chromosomes by HTP-1/2 and LAB-1. Mutating the N terminus of HTP-1 causes ectopic H3 T3 phosphorylation, triggering precocious SCC release without impairing earlier HTP-1 roles in homolog pairing and recombination. CDK-1 exerts temporal regulation of Aurora B recruitment, coupling REC-8 phosphorylation to oocyte maturation. Our findings elucidate a complex regulatory network that uses chromosome axis components, H3 T3 phosphorylation, and cell cycle regulators to ensure accurate chromosome segregation during oogenesis. During meiosis, step-wise release of sister chromatid cohesion mediated by REC-8 cohesin is required for the formation of haploid gametes. Here, the authors show that in C. elegans oocytes, regulated recruitment of Aurora B kinase ensures the correct distribution of REC-8 phosphorylation, which promotes cohesion release.

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