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

Sheona P. Drummond, Katherine Lee 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

Nuclear Pore
Nuclear Envelope
Tail
Dilatation
Membrane Fusion
Cell Nucleus Active Transport
Xenopus
Anti-Idiotypic Antibodies
Membrane Proteins
Cytoplasm
Peptides
Membranes
Growth

Keywords

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

ASJC Scopus subject areas

  • Cell Biology

Cite this

Interference with the cytoplasmic tail of gp210 disrupts "close apposition" of nuclear membranes and blocks nuclear pore dilation. / Drummond, Sheona P.; Wilson, Katherine Lee.

In: Journal of Cell Biology, Vol. 158, No. 1, 08.07.2002, p. 53-62.

Research output: Contribution to journalArticle

@article{0ad28bfe27554efeacac7e76d6d700eb,
title = "Interference with the cytoplasmic tail of gp210 disrupts {"}close apposition{"} of nuclear membranes and blocks nuclear pore dilation",
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.",
keywords = "Membrane fusion, Nuclear pore complex, Nucleoporin, Nucleus, Xenopus egg extracts",
author = "Drummond, {Sheona P.} and Wilson, {Katherine Lee}",
year = "2002",
month = "7",
day = "8",
doi = "10.1083/jcb.200108145",
language = "English (US)",
volume = "158",
pages = "53--62",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "1",

}

TY - JOUR

T1 - Interference with the cytoplasmic tail of gp210 disrupts "close apposition" of nuclear membranes and blocks nuclear pore dilation

AU - Drummond, Sheona P.

AU - Wilson, Katherine Lee

PY - 2002/7/8

Y1 - 2002/7/8

N2 - 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.

AB - 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.

KW - Membrane fusion

KW - Nuclear pore complex

KW - Nucleoporin

KW - Nucleus

KW - Xenopus egg extracts

UR - http://www.scopus.com/inward/record.url?scp=0037043334&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037043334&partnerID=8YFLogxK

U2 - 10.1083/jcb.200108145

DO - 10.1083/jcb.200108145

M3 - Article

C2 - 12093788

AN - SCOPUS:0037043334

VL - 158

SP - 53

EP - 62

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 1

ER -