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U2AF Participates in the binding of TAP (NXF1) to mRNA

  1. Author:
    Zolotukhin, A. S.
    Tan, W.
    Bear, J.
    Smulevitch, S.
    Felber, B. K.

  2. Author Address

    NCI, Human Retrovirus Pathogenesis Sect, Basic Res Lab, Ctr Canc Res, NIH, Bldg 535, Rm 110, Frederick, MD 21702 USA. NCI, Human Retrovirus Pathogenesis Sect, Basic Res Lab, Ctr Canc Res, NIH, Frederick, MD 21702 USA. Felber BK NCI, Human Retrovirus Pathogenesis Sect, Basic Res Lab, Ctr Canc Res, NIH, Bldg 535, Rm 110, Frederick, MD 21702 USA.
    1. Year: 2002
  2. Journal: Journal of Biological Chemistry
    1. 277
    2. 6
    3. Pages: 3935-3942
  4. Type of Article: Article
  1. Abstract:

    TAP/NXF1 is a conserved mRNA export receptor serving as a link between messenger ribonucleoproteins (mRNPs) and the nuclear pore complex. The mechanism by which TAP recognizes its export substrate is unclear. We show here that TAP is added to spliced mRNP in human cells. We identified a distinct region of TAP that targets it to mRNP. Using yeast two-hybrid screens and in vitro binding studies, we found that this, region coincides with a direct binding site for U2AF35, the small subunit of the splicing factor U2AF. This interaction is evolutionarily conserved across metazoa, indicating its significance. We further found in human cells that the exogenously expressed large U2AF subunit, U2AF65, accumulates in spliced mRNP, leading to the recruitment of U2AF35 and TAP. Similarly to TAP, U2AF65 stimulated directly the nuclear export and expression,of an mRNA that is otherwise retained in the nucleus. Together with our finding that U2AF is continuously exported from the nucleus, these data suggest that U2AF participates in nuclear export, by facilitating TAP's addition to its mRNA substrates.

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