JCB logo
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online
doi:10.1083/jcb.1787iti4
The Journal of Cell Biology, Vol. 178, No. 7, 1095-
The Rockefeller University Press, 0021-9525 $30.00
© Leslie
This Article
Right arrow Full Text (PDF, 971K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Leslie, M.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Leslie, M.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

In This Issue

Going their own way in the NPC



Figure 1
Removing certain FG domains disrupts mRNA export (top row) or protein import (bottom row), but not both.

There's more than one way to pass through a nuclear pore, as Terry and Wente show. Different cargos follow different routes through the channels, suggesting a new mechanism for regulating import and export.

A nuclear pore is a bit like a high school hallway, with molecules and their carriers crowding through in both directions. As they make the crossing, carriers attach to sections of pore proteins (Nups) that harbor repeated stretches of phenylalanine and glycine. How binding to these FG repeat domains helps usher cargos through the pores remains controversial.

Three years ago, Wente's group tested the importance of particular FG repeats by making yeast mutants with different combinations of the domains excised. They found that transport doesn't require FG repeats in the filaments that protrude into the cytoplasm and into the basket that hangs from the nuclear side.

To pin down which FG segments are essential, Terry and Wente continued the research with new mutants. The scientists tracked how the loss of certain domains affected mRNA export from the nucleus and protein import via Kapß carriers. If the removal of an FG domain blocked mRNA from exiting, it didn't necessarily prevent Kapß cargos from entering, and vice versa. This difference indicates that the two types of cargos follow different paths through the pore. Cells might be able to control what goes in and out by altering FG domains in specific Nups. Formula

Reference:

Terry, L.J., and S.R. Wente. 2007. J. Cell Biol. 178:1121–1132.[Abstract/Free Full Text]



Mitch Leslie

mitchleslie{at}comcast.net


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 Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?



This Article
Right arrow Full Text (PDF, 971K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Leslie, M.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Leslie, M.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?


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