JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online September 17, 2007
doi:10.1083/jcb.200704174
The Journal of Cell Biology, Vol. 178, No. 7, 1121-1132
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Terry et al.
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 2045K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
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 Terry, L. J.
Right arrow Articles by Wente, S. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Terry, L. J.
Right arrow Articles by Wente, S. R.
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?

Article

Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex



Laura J. Terry and Susan R. Wente

Department of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232

Correspondence to Susan R. Wente: susan.wente{at}vanderbilt.edu

Trafficking of nucleic acids and large proteins through nuclear pore complexes (NPCs) requires interactions with NPC proteins that harbor FG (phenylalanine-glycine) repeat domains. Specialized transport receptors that recognize cargo and bind FG domains facilitate these interactions. Whether different transport receptors utilize preferential FG domains in intact NPCs is not fully resolved. In this study, we use a large-scale deletion strategy in Saccharomyces cerevisiae to generate a new set of more minimal pore (mmp) mutants that lack specific FG domains. A comparison of messenger RNA (mRNA) export versus protein import reveals unique subsets of mmp mutants with functional defects in specific transport receptors. Thus, multiple functionally independent NPC translocation routes exist for different transport receptors. Our global analysis of the FG domain requirements in mRNA export also finds a requirement for two NPC substructures—one on the nuclear NPC face and one in the NPC central core. These results pinpoint distinct steps in the mRNA export mechanism that regulate NPC translocation efficiency.

Abbreviations used in this paper: cNLS, classic NLS; Kap, karyopherin; MBP, maltose-binding protein; mmp, more minimal pore; mRNP, messenger RNP; NE, nuclear envelope; NES, nuclear export sequence; NLS, nuclear localization signal; NPC, nuclear pore complex; Nup, nucleoporin; SC, synthetic complete.


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

Going their own way in the NPC
Mitch Leslie
J. Cell Biol. 2007 178: 1095. [Full Text] [PDF]



This article has been cited by other articles:



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