Nucleocytoplasmic transport is mediated by the interplay between soluble transport factors and nucleoporins resident within the nuclear pore complex (NPC). Understanding this process demands knowledge of components of both the soluble and stationary phases and the interface between them. Here, we provide evidence that Nup2p, previously considered to be a typical yeast nucleoporin that binds import- and export-bound karyopherins, dynamically associates with the NPC in a Ran-facilitated manner. When bound to the NPC, Nup2p associates with regions corresponding to the nuclear basket and cytoplasmic fibrils. On the nucleoplasmic face, where the Ran–GTP levels are predicted to be high, Nup2p binds to Nup60p. Deletion of NUP60 renders Nup2p nucleoplasmic and compromises Nup2p-mediated recycling of Kap60p/Srp1p. Depletion of Ran–GTP by metabolic poisoning, disruption of the Ran cycle, or in vitro by cell lysis, results in a shift of Nup2p from the nucleoplasm to the cytoplasmic face of the NPC. This mobility of Nup2p was also detected using heterokaryons where, unlike nucleoporins, Nup2p was observed to move from one nucleus to the other. Together, our data support a model in which Nup2p movement facilitates the transition between the import and export phases of nucleocytoplasmic transport.
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25 June 2001
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June 25 2001
Nup2p Dynamically Associates with the Distal Regions of the Yeast Nuclear Pore Complex
David J. Dilworth,
David J. Dilworth
aInstitute for Systems Biology, Seattle, Washington, 98105
bDepartment of Cell Biology, University of Alberta, Edmonton, Canada, T6G 2H7
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Adisetyantari Suprapto,
Adisetyantari Suprapto
cThe Rockefeller University, New York, New York, 10021
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Julio C. Padovan,
Julio C. Padovan
cThe Rockefeller University, New York, New York, 10021
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Brian T. Chait,
Brian T. Chait
cThe Rockefeller University, New York, New York, 10021
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Richard W. Wozniak,
Richard W. Wozniak
bDepartment of Cell Biology, University of Alberta, Edmonton, Canada, T6G 2H7
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Michael P. Rout,
Michael P. Rout
bDepartment of Cell Biology, University of Alberta, Edmonton, Canada, T6G 2H7
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John D. Aitchison
John D. Aitchison
aInstitute for Systems Biology, Seattle, Washington, 98105
bDepartment of Cell Biology, University of Alberta, Edmonton, Canada, T6G 2H7
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David J. Dilworth
aInstitute for Systems Biology, Seattle, Washington, 98105
bDepartment of Cell Biology, University of Alberta, Edmonton, Canada, T6G 2H7
Adisetyantari Suprapto
cThe Rockefeller University, New York, New York, 10021
Julio C. Padovan
cThe Rockefeller University, New York, New York, 10021
Brian T. Chait
cThe Rockefeller University, New York, New York, 10021
Richard W. Wozniak
bDepartment of Cell Biology, University of Alberta, Edmonton, Canada, T6G 2H7
Michael P. Rout
bDepartment of Cell Biology, University of Alberta, Edmonton, Canada, T6G 2H7
John D. Aitchison
aInstitute for Systems Biology, Seattle, Washington, 98105
bDepartment of Cell Biology, University of Alberta, Edmonton, Canada, T6G 2H7
Abbreviations used in this paper: cNLS, classical NLS; FG-nup, phenylalanine–glycine repeat nucleoporin; GFP, green fluorescent protein; GST, glutathione S-transferase; IEM, immunoelectron microscopy; kap, karyopherin; NE, nuclear envelope; NES, nuclear export signal; NLS, nuclear localization signal; NPC, nuclear pore complex; pA, protein A; RBD, Ran binding domain.
Received:
January 31 2001
Revision Requested:
April 17 2001
Accepted:
April 19 2001
Online ISSN: 1540-8140
Print ISSN: 0021-9525
© 2001 The Rockefeller University Press
2001
The Rockefeller University Press
J Cell Biol (2001) 153 (7): 1465–1478.
Article history
Received:
January 31 2001
Revision Requested:
April 17 2001
Accepted:
April 19 2001
Citation
David J. Dilworth, Adisetyantari Suprapto, Julio C. Padovan, Brian T. Chait, Richard W. Wozniak, Michael P. Rout, John D. Aitchison; Nup2p Dynamically Associates with the Distal Regions of the Yeast Nuclear Pore Complex. J Cell Biol 25 June 2001; 153 (7): 1465–1478. doi: https://doi.org/10.1083/jcb.153.7.1465
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