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USP7 deubiquitinates RNF2. 7 / 7
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"In order to confirm that USP7 mediates the deubiquitination of RING1B, we added to self ubiquitinated RING1B bacterially expressed purified His 6 -USP7 and its inactive mutant His 6 -USP7 C223S."

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"Although, USP7 directly and specifically deubiquitinates RING1B in vitro and in vivo, it does not discriminate between the activating and proteolysis targeting modes of ubiquitination, and therefore has a stabilizing effect on RING1B."

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"USP7 deubiquitinates ubiquitinated (by itself or external ligase such as E6AP) RING1B ligase of the polycomb complex [XREF_BIBR]."

"Here we identify USP7 as a deubiquitinating enzyme that regulates the ubiquitination state of RING1B."

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"Taken together, these data indicate that USP7 specifically deubiquitinates RING1B in vitro."

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"As shown in Fig. 4 C, USP7 is not a chain type specific DUB and it can deubiquitinate different lysine based polyubiquitin chains.Based on our observation that USP7 can reverse E6-AP-mediated ubiquiti[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"It is possible that in wild type spermatocytes, USP7 may directly deubiquitinate RNF2 and thus reduce H2A ubiquitination in the XY body."