IndraLab

Statements


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"Rpn11, Ubp6 and Uch37 can independently perform their functions and degrade the substrate protein ubiquitin chain in different ways which depend on the length, number and connection type of the ubiquitin chain."

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"After transfecting individual plasmids into cells, we found that ectopic PSMD14 substantially decreased K48-linked and K63-linked ubiquitin on CARM1 but did not affect K11-linked ubiquitin on CARM1 (Fig. 3E)."

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"Rpn11 completely eliminates ubiquitin modification by hydrolyzing the heteropeptide bond between the lysine of substrate protein and the C-terminus of the first ubiquitin [47]."

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"PSMD14 can reduce DNA–ubiquitin conjugates and maintain embryonic stem cell pluripotency and self-renewal abilities (Buckley et al., 2012)."

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"USP44, USP17L2/DUB3, USP11, ZUFSP and POH1 loss promotes the excessive spreading of Ub at DSBs and concomitant excessive accumulation of 53BP1 [57–65]."

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"Depletion of POH1, a DUB and proteasome subunit, prevents removal of ubiquitin from the core of DSB foci, whereas depletion of both POH1 and RAP80 enables ubiquitin to be removed, consistent with the model that RAP80 preserves polyubiquitin modifications on chromatin [XREF_BIBR]."

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"Attenuation of the ubiquitin conjugate DNA damage signal by the proteasomal DUB POH1."

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"RAP80 and ubiquitin chains persist at the IRIF core in POH1 depleted cells, but the ubiquitin chains are removed from the IRIF core when POH1 and RAP80 are simultaneously depleted [XREF_BIBR], suggesting that DUBs but not POH1 degrade ubiquitin chains."

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"In addition to an influence on global Ub conjugates, we found the enzymatic activity of POH1 was also required to restrict Ub accumulation at sites of DNA damage following HU and irradiation (IR)."