Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-11108
Cell 2000 Apr 14;1012:187-98. doi: 10.1016/S0092-8674(00)80829-6.
Show Gene links Show Anatomy links

PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation.

Ohno M , Segref A , Bachi A , Wilm M , Mattaj IW .


???displayArticle.abstract???
In metazoa, assembly of spliceosomal U snRNPs requires nuclear export of U snRNA precursors. Export depends upon the RNA cap structure, nuclear cap-binding complex (CBC), the export receptor CRM1/Xpo1, and RanGTP. These components are however insufficient to support U snRNA export. We identify PHAX (phosphorylated adaptor for RNA export) as the additional factor required for U snRNA export complex assembly in vitro. In vivo, PHAX is required for U snRNA export but not for CRM1-mediated export in general. PHAX is phosphorylated in the nucleus and then exported with RNA to the cytoplasm, where it is dephosphorylated. PHAX phosphorylation is essential for export complex assembly while its dephosphorylation causes export complex disassembly. The compartmentalized PHAX phosphorylation cycle can contribute to the directionality of export.

???displayArticle.pubmedLink??? 10786834
???displayArticle.link??? Cell


Species referenced: Xenopus
Genes referenced: phax xpo1