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A Cell Free Assay to Study Chromatin Decondensation at the End of Mitosis
Published on: December 19, 2015
Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis
Bernhard Hampoelz1, Andre Schwarz2, Paolo Ronchi3
1European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany; Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Abstract:
The molecular events that direct nuclear pore complex (NPC) assembly toward nuclear envelopes have been conceptualized in two pathways that occur during mitosis or interphase, respectively. In gametes and embryonic cells, NPCs also occur within stacked cytoplasmic membrane sheets, termed annulate lamellae (AL), which serve as NPC storage for early development. The mechanism of NPC biogenesis at cytoplasmic membranes remains unknown. Here, we show that during Drosophila oogenesis, Nucleoporins condense into different precursor granules that interact and progress into NPCs. Nup358 is a key player that condenses into NPC assembly platforms while its mRNA localizes to their surface in a translation-dependent manner. In concert, Microtubule-dependent transport, the small GTPase Ran and nuclear transport receptors regulate NPC biogenesis in oocytes. We delineate a non-canonical NPC assembly mechanism that relies on Nucleoporin condensates and occurs away from the nucleus under conditions of cell cycle arrest.
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