Mechanisms of mRNA export

摘要

As mRNA-protein complexes are exported from the nucleus to the cytoplasm, they pass through the nuclear pore complex (NPC). Dbp5, an RNA helicase associated with the NPC through the Nup159 subunit, remodels such complexes. Montpetit et al. present the structure of Dbp5 bound to Glel and the small molecule activator InsP_6, with and without Nup 159 and RNA. Similarities to the structure of the translation initiation complex eIF4G-eIF4A suggest that GlelInsP6 activates Dbp5 by relieving an autoinhibitory mechanism, by promoting RNA release, and (with Nupl59) by stabilizing a conformation that cannot bind RNA.