IndraLab

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USP34 deubiquitinates PIN1. 7 / 7
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"Pin1 is deubiquitinated and stabilized by USP34 in GSCs."
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"Moreover, disruption of USP34 dramatically elevated poly-ubiquitination of Pin1 in GSCs (Fig. 1h, Supplementary Fig. 1f)."
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"Therefore, these data indicate that USP34 deubiquitinates and stabilizes Pin1 proteins."
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"In summary, these data demonstrate that USP34 deubiquitinates and stabilizes Pin1 in GSCs."
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"Here we demonstrate that Pin1 is deubiquitinated and stabilized by USP34, which promotes isomerization of the sole SUMO E2 enzyme Ubc9, leading to SUMO1-modified hypersumoylation to support GSC maintenance."
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"Disruption of USP34 or inhibition of Plk1 promotes poly-ubiquitination and degradation of Pin1."
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"We have shown that Pin1 is deubiquitinated and stabilized by USP34 in GSCs, resulting in the Pin1-catalyzed Ubc9 isomerization and the consequent SUMO1-modified hypersumoylation that are critical for GSC maintenance."
38167292