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Vol. 15, Issue 4, 1991-2002, April 2004

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Distinct Functional Domains within Nucleoporins Nup153 and Nup98 Mediate Transcription-dependent Mobility

Eric R. Griffis ^* , Branch Craige ^* , Christian Dimaano , Katharine S. Ullman , and Maureen A. Powers ^* 

^* Emory University School of Medicine, Department of Cell Biology, Atlanta, Georgia 30322-1100; Emory University Graduate Division of Biomedical and Biological Sciences, Atlanta, Georgia 30322-1100; and Huntsman Cancer Institute, University of Utah, Department of Oncological Sciences, Salt Lake City, Utah 84112

Submitted October 17, 2003; Revised December 5, 2003; Accepted December 8, 2003
Monitoring Editor: Joseph Gall

Despite the apparent overall structural stability of the nuclear pore complex during interphase, at least two nucleoporins have been shown to move dynamically on and off the pore. It is not yet certain what contribution nucleoporin mobility makes to the process of nuclear transport or how such mobility is regulated. Previously, we showed that Nup98 dynamically interacts with the NPC as well as bodies within the nucleus in a transcription-dependent manner. We have extended our studies of dynamics to include Nup153, another mobile nucleoporin implicated in RNA export. In both cases, we found that although only one domain is essential for NPC localization, other regions of the protein significantly affect the stability of association with the pore. Interestingly, like Nup98, the exchange of Nup153 on and off the pore is inhibited when transcription by Pol I and Pol II is blocked. We have mapped the regions required to link Nup98 and Nup153 mobility to transcription and found that the requirements differ depending on which polymerases are inhibited. Our data support a model whereby transcription of RNA is coupled to nucleoporin mobility, perhaps ultimately linking transport of RNAs to a cycle of remodeling at the nuclear pore basket.

Corresponding author. E-mail address: mpowers{at}cellbio.emory.edu.

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