A molecular link between SR protein dephosphorylation and mRNA export | Zendy

Yingqun Huang | Zendy; Therese A. Yario | Zendy; Joan A. Steitz | Zendy

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A molecular link between SR protein dephosphorylation and mRNA export

Author(s) -

Yingqun Huang,

Therese A. Yario,

Joan A. Steitz

Publication year - 2004

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.0403533101

Subject(s) - sr protein , messenger rna , rna splicing , dephosphorylation , nuclear export signal , phosphorylation , microbiology and biotechnology , biology , rna binding protein , alternative splicing , precursor mrna , rna , gene , cell nucleus , biochemistry , phosphatase , cytoplasm

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.

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