Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

A Molecular Link between SR Protein Dephosphorylation and mRNA Export

Yingqun Huang, Therese A. Yario and Joan A. Steitz
Proceedings of the National Academy of Sciences of the United States of America
Vol. 101, No. 26 (Jun. 29, 2004), pp. 9666-9670
Stable URL: http://www.jstor.org/stable/3372514
Page Count: 5
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
A Molecular Link between SR Protein Dephosphorylation and mRNA Export
Preview not available

Abstract

In metazoans, multiple RNA-binding proteins, including the shuttling serine/arginine-rich (SR)-splicing factors, function as adapters for mRNA nuclear export by interacting with the export receptor TAP/nuclear export factor 1 (NXF1). Yet, it is unclear how interactions between adapters and TAP are regulated. Here, we demonstrate that the SR proteins 9G8 and ASF/SF2 exhibit higher affinity for TAP/NXF1 when hypophosphorylated. 9G8 is recruited to the pre-mRNA in a hyperphosphorylated form but becomes hypophosphorylated during splicing both in vivo and in vitro. TAP preferentially binds spliced mRNA-protein complexes compared with pre-mRNA-protein complexes. Thus, the phosphorylation state of the SR protein adapters may underlie the selectivity of TAP-mediated export of spliced mRNA.

Page Thumbnails

  • Thumbnail: Page 
[9666]
    [9666]
  • Thumbnail: Page 
9667
    9667
  • Thumbnail: Page 
9668
    9668
  • Thumbnail: Page 
9669
    9669
  • Thumbnail: Page 
9670
    9670