Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 31626769.
- Also identified by DOI 10.1016/j.cell.2019.09.022 and PMC identifier 6838685.
- Licence recorded as CC BY-NC-ND.
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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.
Medical subject headings
- Drosophila Proteins
- Molecular Chaperones
- Nuclear Pore
- Nuclear Pore Complex Proteins
- Oogenesis