Interference with the cytoplasmic tail of gp210 disrupts "close apposition" of nuclear membranes and blocks nuclear pore dilation

Sheona P. Drummond, Katherine L. Wilson

Research output: Contribution to journalArticle

Abstract

We tested the hypothesis that gp210, an integral membrane protein of nuclear pore complexes (NPCs), mediates nuclear pore formation. Gp210 has a large lumenal domain and small COOH-terminal tail exposed to the cytoplasm. We studied the exposed tail. We added recombinant tail polypeptides to Xenopus nuclear assembly extracts, or inhibited endogenous gp210 tails using anti-tail antibodies. Both strategies had no effect on the formation of fused flattened nuclear membranes, but blocked NPC assembly and nuclear growth. Inhibited nuclei accumulated gp210 and some nucleoporin p62, but failed to incorporate nup214/CAN, nup153, or nup98 and were defective for nuclear import of lamin B3. Scanning and transmission EM revealed a lack of "closely apposed" inner and outer membranes, and the accumulation of novel arrested structures including "mini-pores." We conclude that gp210 has early roles in nuclear pore formation, and that pore dilation is mediated by gp210 and its tail-binding partner(s). We propose that membrane fusion and pore dilation are coupled, acting as a mechanism to control nuclear pore size.

Original languageEnglish (US)
Pages (from-to)53-62
Number of pages10
JournalJournal of Cell Biology
Volume158
Issue number1
DOIs
StatePublished - Jul 8 2002

    Fingerprint

Keywords

  • Membrane fusion
  • Nuclear pore complex
  • Nucleoporin
  • Nucleus
  • Xenopus egg extracts

ASJC Scopus subject areas

  • Cell Biology

Cite this