IndraLab

Statements

USP15 activates REST. 8 / 11
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"While USP15 does not antagonize beta-TrCP-mediated REST degradation, is required for the rapid replenishment of REST upon mitotic exit for the beginning of the new cell cycle."
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"We show that USP15 does not antagonize degradation of pre-existing REST or protect phosphorylated REST at mitosis."
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"DUBs " found in translation " : USP15 controls stability of newly synthesized REST."
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"Instead, the physiological role of USP15 is to promote new REST synthesis to restore its cellular level at mitotic exit."
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"To establish whether the deubiquitylase activity of USP15 could rescue REST, we employed HEK-293T cells, which, unlike A549 cells, are amenable to high efficiency plasmid transfection."
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"The other key observation was that in conditions where translation was inhibited, USP15 knockdown failed to accelerate REST degradation."
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"Through reversing the ubiquitylation of newly synthesized REST, USP15 allows nuclear REST to be replenished in early G 1 after mitotic exit."
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"Depletion of USP15 failed to accelerate the turnover of REST under conditions where translation was inhibited (XREF_FIG)."
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