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PMID: 11950939 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Nup98 is a mobile nucleoporin with transcription-dependent dynamics.

Molecular biology of the cell ·Vol. 13 ·No. 4 ·2002-04-00 ·Pages 1282-97

Griffis ER, Altan N, Lippincott-Schwartz J, Powers MA

Abstract

Nucleoporin 98 (Nup98), a glycine-leucine-phenylalanine-glycine (GLFG) amino acid repeat-containing nucleoporin, plays a critical part in nuclear trafficking. Injection of antibodies to Nup98 into the nucleus blocks the export of most RNAs. Nup98 contains binding sites for several transport factors; however, the mechanism by which this nucleoporin functions has remained unclear. Multiple subcellular localizations have been suggested for Nup98. Here we show that Nup98 is indeed found both at the nuclear pore complex and within the nucleus. Inside the nucleus, Nup98 associates with a novel nuclear structure that we term the GLFG body because the GLFG domain of Nup98 is required for targeting to this structure. Photobleaching of green fluorescent protein-Nup98 in living cells reveals that Nup98 is mobile and moves between these different localizations. The rate of recovery after photobleaching indicates that Nup98 interacts with other, less mobile, components in the nucleoplasm. Strikingly, given the previous link to nuclear export, the mobility of Nup98 within the nucleus and at the pore is dependent on ongoing transcription by RNA polymerases I and II. These data give rise to a model in which Nup98 aids in direction of RNAs to the nuclear pore and provide the first potential mechanism for the role of a mobile nucleoporin.

MeSH Terms
Animals Binding Sites Cells, Cultured DNA, Complementary/metabolism Glycine/chemistry Green Fluorescent Proteins HeLa Cells Humans Leucine/chemistry Luminescent Proteins/metabolism Microscopy, Electron Microscopy, Fluorescence Nuclear Pore Complex Proteins/metabolism,physiology Protein Binding RNA/metabolism RNA Polymerase I/metabolism RNA Polymerase II/metabolism Time Factors Transcription, Genetic Transfection Xenopus
Chemicals
DNA, Complementary Luminescent Proteins Nuclear Pore Complex Proteins nuclear pore complex protein 98 Green Fluorescent Proteins RNA RNA Polymerase II RNA Polymerase I Leucine Glycine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Griffis Eric R
Department of Cell Biology, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
Altan Nihal
Lippincott-Schwartz Jennifer
Powers Maureen A
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
Published
2002-04-00
Pages
1282-97
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC102269
Subset
IM
Grants
NIGMS NIH HHS · R01 GM059975 · United States
NIGMS NIH HHS · GM-59975 · United States
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