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.
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8 July 2002
Article|
July 01 2002
Interference with the cytoplasmic tail of gp210 disrupts “close apposition” of nuclear membranes and blocks nuclear pore dilation
Sheona P. Drummond,
Sheona P. Drummond
Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205
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Katherine L. Wilson
Katherine L. Wilson
Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205
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Sheona P. Drummond
Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205
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: [email protected]
The online version of this article includes supplemental material.
S.P. Drummond's present address is Department of Structural Cell Biology, Paterson Institute for Cancer Research, Christie Hospital, Wilmslow Road, Manchester M20 9BX, UK.
*
Abbreviations used in this paper: GST, glutathione-S-transferase; HA, hemagglutinin; NIB, nuclear isolation buffer; NPC, nuclear pore complex; SEM, scanning EM; TEM, transmission EM.
Received:
August 29 2001
Revision Received:
May 16 2002
Accepted:
May 20 2002
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2002
J Cell Biol (2002) 158 (1): 53–62.
Article history
Received:
August 29 2001
Revision Received:
May 16 2002
Accepted:
May 20 2002
Citation
Sheona P. Drummond, Katherine L. Wilson; Interference with the cytoplasmic tail of gp210 disrupts “close apposition” of nuclear membranes and blocks nuclear pore dilation . J Cell Biol 8 July 2002; 158 (1): 53–62. doi: https://doi.org/10.1083/jcb.200108145
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