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A Nucleoporin Docks Protein Phosphatase 1 to Direct Meiotic Chromosome Segregation and Nuclear Assembly

By Neil Hattersley, Dhanya Cheerambathur, Mark Moyle, Marine Stefanutti, Amelia Richardson, Kian-Yong Lee, Julien Dumont, Karen Oegema and Arshad Desai


International audienceDuring M-phase entry in metazoans with open mitosis, the concerted action of mitotic kinases disassembles nuclei and promotes assembly of kinetochores—the primary microtubule attachment sites on chromosomes. At M-phase exit, these major changes in cellular architecture must be reversed. Here, we show that the conserved kinetochore-localized nucleoporin MEL-28/ELYS docks the catalytic subunit of protein phosphatase 1 (PP1c) to direct kinetochore disassembly-dependent chromosome segregation during oocyte meiosis I and nuclear assembly during the transition from M phase to interphase. During oocyte meiosis I, MEL-28-PP1c disassembles kinetochores in a timely manner to promote elongation of the acentrosomal spindles that segregate homologous chromosomes. During nuclear assembly, MEL-28 recruits PP1c to the periphery of decondensed chromatin, where it directs formation of a functional nuclear compartment. Thus, a pool of phosphatase activity associated with a kinetochore-localized nucleoporin contributes to two key events that occur during M-phase exit in metazoans: kinetochore disassembly and nuclear reassembly

Topics: nuclear pore, ELYS, MEL-28, kinetochore, centromere, meiosis, chromosome segregation, protein phosphatase 1, PP1 docking, nuclear pore assembly, [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology, [ SDV.BDD ] Life Sciences [q-bio]/Development Biology
Publisher: Elsevier
Year: 2016
DOI identifier: 10.1016/j.devcel.2016.08.006
OAI identifier: oai:HAL:hal-01472324v1
Provided by: Hal-Diderot
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