Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis

被引:66
|
作者
Hampoelz, Bernhard [1 ,2 ]
Schwarz, Andre [1 ,3 ]
Ronchi, Paolo [4 ]
Bragulat-Teixidor, Helena [4 ]
Tischer, Christian [5 ]
Gaspar, Imre [6 ]
Ephrussi, Anne [6 ]
Schwab, Yannick [4 ,7 ]
Beck, Martin [1 ,2 ,7 ]
机构
[1] European Mol Biol Lab, Struct & Computat Biol Unit, Heidelberg, Germany
[2] Max Planck Inst Biophys, Frankfurt, Germany
[3] Fac Biosci, Collaborat Joint PhD Degree EMBL & Heidelberg Uni, Heidelberg, Germany
[4] European Mol Biol Lab, Electron Microscopy Core Facil, Heidelberg, Germany
[5] European Mol Biol Lab, Ctr Bioimage Anal, Heidelberg, Germany
[6] European Mol Biol Lab, Dev Biol Unit, Heidelberg, Germany
[7] European Mol Biol Lab, Cell Biol & Biophys Unit, Heidelberg, Germany
基金
欧洲研究理事会;
关键词
BICAUDAL-D; COMPLEX; DROSOPHILA; ENVELOPE; PROTEIN; LOCALIZATION; CHROMATIN; MEMBRANE; RAN; PERMEABILITY;
D O I
10.1016/j.cell.2019.09.022
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:671 / +
页数:33
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