A Nucleoporin Docks Protein Phosphatase 1 to Direct Meiotic Chromosome Segregation and Nuclear Assembly.
During 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.
Department of Cellular and Molecular Medicine, Ludwig Institute for Cancer Research, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0653, USA.
Neil
N
Hattersley
Department of Cellular and Molecular Medicine, Ludwig Institute for Cancer Research, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0653, USA.
Dhanya
D
Cheerambathur
Department of Cellular and Molecular Medicine, Ludwig Institute for Cancer Research, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0653, USA.
Mark
M
Moyle
Institut Jacques Monod, CNRS, UMR 7592, University Paris Diderot, Sorbonne Paris Cité, 75205 Paris, France.
Marine
M
Stefanutti
Department of Cellular and Molecular Medicine, Ludwig Institute for Cancer Research, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0653, USA.
Amelia
A
Richardson
Department of Cellular and Molecular Medicine, Ludwig Institute for Cancer Research, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0653, USA.
Kian-Yong
KY
Lee
Institut Jacques Monod, CNRS, UMR 7592, University Paris Diderot, Sorbonne Paris Cité, 75205 Paris, France.
Julien
J
Dumont
Department of Cellular and Molecular Medicine, Ludwig Institute for Cancer Research, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0653, USA.
Karen
K
Oegema
Department of Cellular and Molecular Medicine, Ludwig Institute for Cancer Research, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0653, USA. Electronic address: abdesai@ucsd.edu.
Arshad
A
Desai
D000818:Animals; D017173:Caenorhabditis elegans / Q000235:genetics; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism*; D020090:Chromosome Segregation / Q000235:genetics; D004268:DNA-Binding Proteins; D006801:Humans; D018386:Kinetochores / Q000378:metabolism; D008540:Meiosis / Q000235:genetics*; D009685:Nuclear Envelope / Q000235:genetics / Q000378:metabolism*; D028861:Nuclear Pore Complex Proteins / Q000235:genetics / Q000378:metabolism; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D009865:Oocytes / Q000254:growth & development / Q000378:metabolism; D060066:Protein Interaction Maps / Q000235:genetics; D017476:Receptors, Neuropeptide Y / Q000235:genetics / Q000378:metabolism*
D029742:Caenorhabditis elegans Proteins; D004268:DNA-Binding Proteins; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; D017476:Receptors, Neuropeptide Y; C514979:mel-28 protein, C elegans; C109491:neuropeptide Y4 receptor
ELYS; MEL-28; PP1 docking; centromere; chromosome segregation; kinetochore; meiosis; nuclear pore; nuclear pore assembly; protein phosphatase 1