IndraLab

Statements

USP2 activates Ubiquitin. 6 / 7
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"At the molecular level, the simplest explanation for this result is that USP2 drives the Ub K48 -Imd molecules to the proteasome and/or ensures the removal of Ub K48 from Imd at the level of the proteasome, then allowing for Imd degradation by the proteasome machinery."
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"As shown in XREF_FIG, USP2, a DUB that non specifically targets all ubiquitin linkages, completely reduced polyubiquitinated TLR2."
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"Moreover, P5091 inhibits USP7-, but not USP2- or USP8 mediated cleavage of poly K48 linked ubiquitin chains (visualized by the presence or absence of mono-ubiquitin) (XREF_SUPPLEMENTARY)."
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"In agreement with this interpretation, no cleavage was detected if USP2 was allowed to remove ubiquitin chains prior to DDI2-RAD23 incubation, showing that DDI2 requires the ubiquitin chain yet cleaves in the body of the NRF1 protein (Figure 4A, compare lanes 17–20 with 11–14)."
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"USP2 promotes stabilization of cyclinD1 via direct interaction with cyclin D1 and antagonizes ubiquitin dependent degradation (Shan et al., 2009)."
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"The specificity of SJB was confirmed by various experiments : first, we show that SJB potently and selectively block USP1 activity without inhibiting other DUBs (USP2/USP5/USP7/USP14/UCH37); second, SJB inhibited binding of USP1 with HA-Ub-VS probe, but it did not affect labeling of other DUBs with probe; and third, SJB inhibited USP1, but not USP2 or USP7, triggered cleavage of ubiquitin tetramer chains."
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