Journal
TRENDS IN CELL BIOLOGY
Volume 15, Issue 3, Pages 121-124Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2005.01.005
Keywords
-
Categories
Ask authors/readers for more resources
CRM1 mediates the nuclear export of proteins exposing leucine-rich nuclear-export signals (NESs). Most NESs bind to CRM1 with relatively low affinity. Recently, higher-affinity NESs were selected from a 15-mer random peptide library. Unexpectedly, complexes between high-affinity NESs and CRM1 accumulate at the cytoplasmic filaments of the nuclear pore complex (NPC). This finding suggests that high-affinity NES binding to CRM1 impairs the efficient release of export complexes from the NPC, explaining why leucine-rich NESs have evolved to be weak.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available