![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
|
|
|
|
|
||
A more recent version of this article appeared on April 1, 2004
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on October 17, 2003
Revised on December 5, 2003
Accepted on December 8, 2003
1 Emory University School of Medicine, Department of Cell Biology, Emory University Graduate Division of Biomedical and Biological Sciences
2 Huntsman Cancer Institute, University of Utah, Department of Oncological Sciences
3 Emory University School of Medicine, Department of Cell Biology
* Corresponding author. E-mail address: mpowers{at}cellbio.emory.edu.
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 upon 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.
This article has been cited by other articles:
|
|
 |
|
  M. Khacho, K. Mekhail, K. Pilon-Larose, A. Pause, J. Cote, and S. Lee eEF1A Is a Novel Component of the Mammalian Nuclear Protein Export Machinery Mol. Biol. Cell, December 1, 2008; 19(12): 5296 - 5308. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. A. Ratner, A. E. Hodel, and M. A. Powers Molecular Determinants of Binding between Gly-Leu-Phe-Gly Nucleoporins and the Nuclear Pore Complex J. Biol. Chem., November 23, 2007; 282(47): 33968 - 33976. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. R. Ball, C. Dimaano, A. Bilak, E. Kurchan, M. T. Zundel, and K. S. Ullman Sequence Preference in RNA Recognition by the Nucleoporin Nup153 J. Biol. Chem., March 23, 2007; 282(12): 8734 - 8740. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Soop, B. Ivarsson, B. Bjorkroth, N. Fomproix, S. Masich, V. C. Cordes, and B. Daneholt Nup153 Affects Entry of Messenger and Ribosomal Ribonucleoproteins into the Nuclear Basket during Export Mol. Biol. Cell, December 1, 2005; 16(12): 5610 - 5620. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Krull, J. Thyberg, B. Bjorkroth, H.-R. Rackwitz, and V. C. Cordes Nucleoporins as Components of the Nuclear Pore Complex Core Structure and Tpr as the Architectural Element of the Nuclear Basket Mol. Biol. Cell, September 1, 2004; 15(9): 4261 - 4277. [Abstract] [Full Text] [PDF]
|
|
