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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
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3372514
Page Count: 5
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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.
Proceedings of the National Academy of Sciences of the United States of America © 2004 National Academy of Sciences