Two closely related human nuclear export factors utilize entirely distinct export pathways.

Journal Article (Journal Article)

Nuclear mRNA export mediated by the human protein TAP requires a carboxy-terminal domain that directly interacts with components of the nuclear pore complex. Here we demonstrate that NXF3, a human RNA binding protein related to TAP, lacks this domain yet retains the ability to export tethered RNA transcripts and to shuttle between the nucleus and the cytoplasm. NXF3 contains a novel Crm1-dependent nuclear export signal that compensates in cis for the loss of the nuclear pore targeting domain. NXF3-dependent RNA export is therefore blocked by Crm1-specific inhibitors that do not affect TAP function. Thus, while the related TAP and NXF3 proteins are both capable of mediating nuclear RNA export, they do so via unrelated export pathways.

Full Text

Duke Authors

Cited Authors

  • Yang, J; Bogerd, HP; Wang, PJ; Page, DC; Cullen, BR

Published Date

  • August 2001

Published In

Volume / Issue

  • 8 / 2

Start / End Page

  • 397 - 406

PubMed ID

  • 11545741

International Standard Serial Number (ISSN)

  • 1097-2765

Digital Object Identifier (DOI)

  • 10.1016/s1097-2765(01)00303-3


  • eng

Conference Location

  • United States