Quality control of spliced mRNAs requires the shuttling SR proteins Gbp2 and Hrb1.

Eukaryotic cells have to prevent the export of unspliced pre-mRNAs until intron removal is completed to avoid the expression of aberrant and potentially harmful proteins. Only mature mRNAs associate with the export receptor Mex67/TAP and enter the cytoplasm. Here we show that the two shuttling serine/arginine (SR)-proteins Gbp2 and Hrb1 ...
are key surveillance factors for the selective export of spliced mRNAs in yeast. Their absence leads to the significant leakage of unspliced pre-mRNAs into the cytoplasm. They bind to pre-mRNAs and the spliceosome during splicing, where they are necessary for the surveillance of splicing and the stable binding of the TRAMP complex to spliceosome-bound transcripts. Faulty transcripts are marked for their degradation at the nuclear exosome. On correct mRNAs the SR proteins recruit Mex67 upon completion of splicing to allow a quality controlled nuclear export. Altogether, these data identify a role for shuttling SR proteins in mRNA surveillance and nuclear mRNA quality control.
Mesh Terms:
Active Transport, Cell Nucleus, Cell Nucleus, Gene Deletion, Models, Biological, Mutant Proteins, Nucleocytoplasmic Transport Proteins, Poly(A)-Binding Proteins, Protein Binding, Proteolysis, RNA Precursors, RNA Splicing, RNA, Messenger, RNA-Binding Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Spliceosomes
Nat Commun
Date: Jan. 24, 2014
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