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Molecular and Cellular Biology, January 2003, p. 534-542, Vol. 23, No. 2
0270-7306/03/$08.00+0 DOI: 10.1128/MCB.23.2.534-542.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Binding Dynamics of Structural Nucleoporins Govern Nuclear Pore Complex Permeability and May Mediate Channel Gating
Nataliya Shulga and David S. Goldfarb*
Department of Biology, University of Rochester, Rochester, New York 14627
Received 7 August 2002/
Returned for modification 12 September 2002/
Accepted 4 October 2002
The nuclear pore complex (NPC) is a permeable sieve that can dilate to facilitate the bidirectional translocation of a wide size range of receptor-cargo complexes. The binding of receptors to FG nucleoporin docking sites triggers channel gating by an unknown mechanism. Previously, we used deoxyglucose and chilling treatments to implicate Nup170p and Nup188p in the control of NPC sieving in Saccharomyces cerevisiae. Here, we report that aliphatic alcohols increase the permeability of wild-type and nup170
NPCs. In conjunction with increases in permeability, aliphatic alcohols, deoxyglucose, and chilling trigger the reversible dissociation of several nucleoporins from nup170
NPCs. These results are consistent with the hypothesis that NPC gating occurs when molecular latches composed of FG repeats and structural nucleoporins dissociate.
* Corresponding author. Mailing address: Department of Biology, University of Rochester, Rochester, NY 14627. Phone: (585) 275-3890. Fax: (585) 275-2070. E-mail:
dasg{at}mail.rochester.edu.
Molecular and Cellular Biology, January 2003, p. 534-542, Vol. 23, No. 2
0022-538X/03/$08.00+0 DOI: 10.1128/MCB.23.2.534-542.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
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