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A more recent version of this article appeared on November 1, 2005
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Submitted on July 18, 2005
Revised on August 16, 2005
Accepted on August 17, 2005
*Section of Life Sciences, Södertörns University College, SE-141 89 Huddinge, Sweden; Department of Biosciences at Novum, Karolinska Institute, SE-141 86 Huddinge, Sweden; Institute of Cytology and Genetics, 630090 Novosibirsk-90, Russia
Monitoring Editor: Karsten Weis
Disassembly and reassembly of the nuclear pore complexes (NPCs) is one of the major events during open mitosis in higher eukaryotes, however how this process controlled by the mitotic machinery is not clear. To investigate this we developed a novel in vivo model system based on syncytial Drosophila embryos. We microinjected different mitotic effectors into the embryonic cytoplasm and monitored the dynamics of disassembly/reassembly of NPCs in live embryos using fluorescently labeled wheat germ agglutinin (WGA) or in fixed embryos using electron microscopy and immunostaing techniques. We found that in live embryos Cdk1 activity was necessary and sufficient to induce disassembly of NPCs as well as their cytoplasmic mimics - annulate lamellae pore complexes (ALPCs). Cdk1 activity was also required for keeping NPCs and ALPCs disassembled during mitosis. In agreement recombinant Cdk1/cyclin B was able to induce phosphorylation and dissociation of nucleoporins from the NPCs in vitro. Conversely, reassembly of NPCs and ALPCs was dependent on the activity of protein phosphatases, sensitive to okadaic acid (OA). Our findings suggest a model where mitotic disassembly/reassembly of the NPCs is regulated by a dynamic equilibrium of Cdk1 and OA-sensitive phosphatase activities, and provide evidence that mitotic phosphorylation mediates disassembly of the NPC.
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