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...

The Rockefeller University Press
2007
The Rockefeller University Press
2007
You do not currently have access to this content.