JCB logo
R&D Systems
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 28 October 2002. doi:10.1083/jcb.200203079
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lusk, C. P.
Right arrow Articles by Wozniak, R. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lusk, C. P.
Right arrow Articles by Wozniak, R. W.
Related Collections
Right arrowRelated Article
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
© The Rockefeller University Press, 0021-9525/2002/10/267 $5.00
The Journal of Cell Biology, Volume 159, Number 2, 267-278

Article

 Karyopherins in nuclear pore biogenesis : a role for Kap121p in the assembly of Nup53p into nuclear pore complexes



C. Patrick Lusk1, Taras Makhnevych1, Marcello Marelli1,2, John D. Aitchison2 and Richard W. Wozniak1

1 Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada
2 Institute for Systems Biology, Seattle, WA 98103

Address correspondence to Richard W. Wozniak, Dept. of Cell Biology, University of Alberta, Edmonton, AB, T6G 2H7 Canada. Tel.: (780) 492-1384. Fax: (780) 492-0450. E-mail: rick.wozniak{at}ualberta.ca

The mechanisms that govern the assembly of nuclear pore complexes (NPCs) remain largely unknown. Here, we have established a role for karyopherins in this process. We show that the yeast karyopherin Kap121p functions in the targeting and assembly of the nucleoporin Nup53p into NPCs by recognizing a nuclear localization signal (NLS) in Nup53p. This karyopherin-mediated function can also be performed by the Kap95p–Kap60p complex if the Kap121p-binding domain of Nup53p is replaced by a classical NLS, suggesting a more general role for karyopherins in NPC assembly. At the NPC, neighboring nucleoporins bind to two regions in Nup53p. One nucleoporin, Nup170p, associates with a region of Nup53p that overlaps with the Kap121p binding site and we show that they compete for binding to Nup53p. We propose that once targeted to the NPC, dissociation of the Kap121p–Nup53p complex is driven by the interaction of Nup53p with Nup170p. At the NPC, Nup53p exists in two separate complexes, one of which is capable of interacting with Kap121p and another that is bound to Nup170p. We propose that fluctuations between these two states drive the binding and release of Kap121p from Nup53p, thus facilitating Kap121p's movement through the NPC.

Key Words: nuclear envelope; nucleoporins; NPC assembly; nuclear transport


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?

Related Article

Initiate then elongate
Alan W. Dove
J. Cell Biol. 2002 159: 198-199. [Full Text] [PDF]



This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents