Publications by authors named "A Roobol"

There is a desire to engineer mammalian host cell lines to improve cell growth/biomass accumulation and recombinant biopharmaceutical protein production in industrially relevant cell lines such as the CHOK1 and HEK293 cell lines. The over-expression of individual subunits of the eukaryotic translation factor eIF3 in mammalian cells has previously been shown to result in oncogenic properties being imparted on cells, including increased cell proliferation and growth and enhanced global protein synthesis rates. Here we report on the engineering of CHOK1 and HEK cells to over-express the eIF3i and eIF3c subunits of the eIF3 complex and the resultant impact on cell growth and a reporter of exogenous recombinant protein production.

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Cooling and hypothermia are profoundly neuroprotective, mediated, at least in part, by the cold shock protein, RBM3. However, the neuroprotective effector proteins induced by RBM3 and the mechanisms by which mRNAs encoding cold shock proteins escape cooling-induced translational repression are unknown. Here, we show that cooling induces reprogramming of the translatome, including the upregulation of a new cold shock protein, RTN3, a reticulon protein implicated in synapse formation.

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Article Synopsis
  • The RNA exosome is crucial for RNA processing and degrading faulty RNAs in eukaryotic cells, but its regulation, especially under stress, is not well understood.
  • Recent findings show that lowering the temperature in mammalian cells affects the expression of EXOSC10, a key component of the RNA exosome, and increases the process of SUMOylation, where small proteins are added to EXOSC10.
  • The study indicates that SUMOylation of EXOSC10 decreases its abundance and is linked to defects in ribosomal RNA processing under cold stress, highlighting a new regulatory mechanism in RNA metabolism.
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Article Synopsis
  • * Mild cooling triggers changes in translation initiation factors and primarily reduces global protein synthesis rates by phosphorylating eEF2, which is controlled by eEF2K.
  • * The activation of eEF2K is largely due to Ca2+ ion release from the endoplasmic reticulum, offering potential avenues to restore protein synthesis and applications in both medical and industrial fields.
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