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USP1 deubiquitinates PARP1. 9 / 9
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"USP1 promotes cholangiocarcinoma progression by deubiquitinating PARP1 to prevent its proteasomal degradation."
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"Firstly, we identify the deubiquitination of PARP1 by USP1 as one of its major targets in CCA."
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"Together, these results confirm that USP1 directly deubiquitinates PARP1.To determine the lysine site of PARP1 targeted by USP1, we conducted a thorough analysis of the ubiquitination-specific mass spectrometry data and observed that Lys-197 may be an important site for USP1 deubiquitination of PARP1 (Fig. 3E)."
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"Together, these data suggested that USP1 deubiquitinates PARP1, but it is not involved in the regulation of its protein stability that, conversely, seems to be linked to the activity of USP15 in triple-negative breast cancer model (22)."
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"We confirmed that USP1 inhibition, alone and better in combination with niraparib, enhanced PARP1 ubiquitination (Fig. 4C and fig."
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"Overall, the data collected here indicated that USP1 activity is necessary to deubiquitinate PARP1 at the site of DNA damage thereby modulating PARP1 dynamic activity necessary for the repair of damaged DNA (Fig. 6I)."
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"USP1 deubiquitinates PARP1 to regulate its trapping and PARylation activity."
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"Moreover, the overexpression of USP1 but not of the inactive form USP1 (9) reduced PARP1 polyubiquitination (Fig. 4A)."
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"It suggests that K197 site is the primary USP1 deubiquitination target on PARP1 controlling its degradation.Poly-ubiquitination chains are generated primarily through two distinct types of bonds: Lys48 or Lys63 chains."
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