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Published online 1 July 2002. doi:10.1083/jcb.200108145
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© The Rockefeller University Press, 0021-9525/2002/7/53 $5.00
The Journal of Cell Biology, Volume 158, Number 1, July 8, 2002 53-62

Article

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

Sheona P. Drummond and Katherine L. Wilson

Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205

Address correspondence to Katherine L. Wilson, Department of Cell Biology, WBSB Room G10, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205. Tel.: (410) 955-1801. Fax: (410) 955-4129. E-mail: klwilson{at}jhmi.edu

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.

Key Words: nucleus; membrane fusion; Xenopus egg extracts; nuclear pore complex; nucleoporin


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