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J. Cell Biol.,
Volume 145, Number 2, April 19, 1999 237-254
* Department of Genetics, St. Jude Children's Research Hospital, Memphis, Tennessee 38105; Gle2p is implicated in nuclear export of
poly(A)+ RNA and nuclear pore complex (NPC)
structure and distribution in Saccharomyces cerevisiae.
Gle2p is anchored at the nuclear envelope (NE) via a
short Gle2p-binding motif within Nup116p called
GLEBS. The molecular mechanism by which Gle2p
and the Gle2p-Nup116p interaction function in mRNA
export is unknown. Here we show that RAE1, the
mammalian homologue of Gle2p, binds to a GLEBS-like NUP98 motif at the NPC through multiple domains that include WD-repeats and a COOH-terminal non-WD-repeat extension. This interaction is direct, as
evidenced by in vitro binding studies and chemical
cross-linking. Microinjection experiments performed in
Xenopus laevis oocytes demonstrate that RAE1 shuttles between the nucleus and the cytoplasm and is exported from the nucleus in a temperature-dependent
and RanGTP-independent manner. Docking of RAE1
to the NE is highly dependent on new mRNA synthesis.
Overexpression of the GLEBS-like motif also inhibits NE binding of RAE1 and induces nuclear accumulation of poly(A)+ RNA. Both effects are abrogated
either by the introduction of point mutations in the
GLEBS-like motif or by overexpression of RAE1, indicating a direct role for RAE1 and the NUP98-RAE1
interaction in mRNA export. Together, our data suggest that RAE1 is a shuttling transport factor that
directly contributes to nuclear export of mRNAs
through its ability to anchor to a specific NUP98 motif at the NPC.
The European Molecular Biology
Laboratory, Heidelberg, Germany D69117; and § Department of Pediatrics & Adolescent Medicine, Mayo Clinic, Rochester,
Minnesota 55905
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