RGD Reference Report - RNA export mediated by tap involves NXT1-dependent interactions with the nuclear pore complex. - Rat Genome Database

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RNA export mediated by tap involves NXT1-dependent interactions with the nuclear pore complex.

Authors: Levesque, L  Guzik, B  Guan, T  Coyle, J  Black, BE  Rekosh, D  Hammarskjold, ML  Paschal, BM 
Citation: Levesque L, etal., J Biol Chem 2001 Nov 30;276(48):44953-62. Epub 2001 Sep 28.
RGD ID: 737638
Pubmed: PMID:11579093   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M106558200   (Journal Full-text)

Nuclear export of ribonucleoprotein complexes requires cis-acting signals and recognition by receptors that mediate translocation through the nuclear pore complex. Translocation is likely to involve a series of physical interactions between the ribonucleoprotein complex and nucleoporins within the nuclear pore complex. Here, we have characterized the function of NXT1 in the context of the Tap-dependent RNA export pathway. Tap has been implicated in the nuclear export of RNA transcripts derived from Mason-Pfizer monkey virus that contain the constitutive transport element. We demonstrate that NXT1 stimulates binding of a Tap-RNA complex to nucleoporins in vitro, and we provide mutational analysis that shows these interactions are necessary for nuclear export of an intron-containing viral mRNA in vivo. Tap contains separate domains for binding to nucleoporins and NXT1, both of which are critical for its export function. RNA export is mediated by a heterodimer of Tap and NXT1, and the function of NXT1 on this pathway is to regulate the affinity of the Tap-RNA complex for nucleoporins within the nuclear pore complex. We propose that NXT1-dependent binding of the Tap-RNA complex to the nucleoporin p62, which we have reconstituted in vitro using recombinant proteins, represents a single step of the translocation reaction.

Objects referenced in this article
Gene Nxf1 nuclear RNA export factor 1 Mus musculus
Gene Nxt1 NTF2-related export protein 1 Mus musculus

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