Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis.

Cell

European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany; Max Planck Institute of Biophysics, Frankfurt am Main, Germany; European Molecular Biology Laboratory, Cell Biology and Biophysics Unit, Heidelberg, Germany. Electronic address:

Published: October 2019

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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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6838685PMC
http://dx.doi.org/10.1016/j.cell.2019.09.022DOI Listing

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