Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis

Cell. 2019 Oct 17;179(3):671-686.e17. doi: 10.1016/j.cell.2019.09.022.

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.

Keywords: NPC assembly; Nup358; RNA localization; Ran; local translation; microtubule-dependent transport; nuclear pore complex; nucleoporin condensation; oogenesis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • Animals
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster
  • Female
  • Microtubules / metabolism
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism*
  • Nuclear Pore / metabolism*
  • Nuclear Pore Complex Proteins / genetics
  • Nuclear Pore Complex Proteins / metabolism*
  • Oogenesis*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • ran GTP-Binding Protein / genetics
  • ran GTP-Binding Protein / metabolism

Substances

  • Drosophila Proteins
  • Molecular Chaperones
  • Nuclear Pore Complex Proteins
  • RNA, Messenger
  • ran-binding protein 2
  • ran GTP-Binding Protein