| Literature DB >> 31626769 |
Bernhard Hampoelz1, Andre Schwarz2, Paolo Ronchi3, Helena Bragulat-Teixidor3, Christian Tischer4, Imre Gaspar5, Anne Ephrussi5, Yannick Schwab6, Martin Beck7.
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.Entities:
Keywords: NPC assembly; Nup358; RNA localization; Ran; local translation; microtubule-dependent transport; nuclear pore complex; nucleoporin condensation; oogenesis
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Year: 2019 PMID: 31626769 PMCID: PMC6838685 DOI: 10.1016/j.cell.2019.09.022
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582