A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm

Article Abstract:

Some human SR proteins stay in the nucleus, but SF2/ASF, SRp20, and 9G8 shuttle rapidly between the nucleus and cytoplasm all of the time. The carboxy-terminal arginine/serine-rich (RS) domain is necessary for shuttling but not adequate for shuttling of an unrelated protein reporter. It seems stable RNA binding mediated by the RNA-recognition motifs may be necessary for shuttling. Different SR proteins have given transport actions in the cell. Shuttling family members may be active not only in nuclear pre-mRNA splicing but also in cytoplasmic events and mRNA transport. They may act in processes that involve nucleus-cytoplasm communication.

Analysis, Cell nuclei, Cell nucleus, RNA splicing, Cytoplasm

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Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1

Article Abstract:

The recruitment and activation of mRNA decay enzymes by two AU-rich elements (AREs) mediated decay activation domains in the proteins tristetraprolin (TTP) and its homolog BRF-1 is examined. The results indicate that the recruitment of mRNA decay enzymes by the TTP protein family acts as a molecular link between ARE-containing mRNAs and the mRNA decay machinery.

All Other Basic Organic Chemical Manufacturing, Enzymes, Other Basic Organic Chemical Manufacturing, Enzymes for Food Processing

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A novel role for shuttling SR proteins in mRNA translation

Article Abstract:

Pre-mRNA splicing, which forms an essential step in gene expression, is catalyzed by large ribonucleoprotein complex and examined. Findings suggest that Ser-Arg-rich (SR) proteins play multiple roles in the metabolism of mRNA in nuclear and cytoplamic compartment of the cell.

Gene expression

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