Accéder au contenu
Merck

Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis.

Cell (2019-10-19)
Bernhard Hampoelz, Andre Schwarz, Paolo Ronchi, Helena Bragulat-Teixidor, Christian Tischer, Imre Gaspar, Anne Ephrussi, Yannick Schwab, Martin Beck
RÉSUMÉ

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.

MATÉRIAUX
Référence du produit
Marque
Description du produit

Sigma-Aldrich
Anti-HA antibody produced in rabbit, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
1,6-Hexanediol, 99%
Sigma-Aldrich
Cycloheximide, Biotechnology Performance Certified
Sigma-Aldrich
D.E.R. 332, used as embedding medium
Sigma-Aldrich
Homoharringtonine, ≥98% (HPLC)