IndraLab

Statements

MKO1 binds PSMD14. 7 / 7
| 7
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"Our results show that PSMD14-mKO1 accumulates in response to local UVC stimulation, but with slower kinetics than DDB2, XPC, and RAD23B. Notably in this regard, the proteasome is one of the most abundant protein factors in a cell, so even weak accumulation may indicate the presence of substantial numbers of molecules at damaged sites."
| PMC
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"PSMD14 fused to the N-terminus of mKO1 (PSMD14-mKO1) was stably expressed in U2OS cells with wild-type, XPC KO , or DDB2 KO background (Fig.  xref d)."
| PMC
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"In these cell lines, PSMD14-mKO1 was overexpressed, whereas expression of endogenous PSMD14 was almost completely suppressed."
| PMC
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"Because these cells proliferated normally, it is likely that ectopically expressed PSMD14-mKO1 displaced the endogenous protein to form functional 19S regulatory particles."
| PMC
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"Under normal culture conditions, PSMD14-mKO1 localized in both the cytoplasm and nucleus (Fig.  xref f and Supplementary Fig. 6a)."
| PMC
sparser
"In these cell lines, we observed recruitment of PSMD14-mKO1 to DNA damage sites, albeit with slower kinetics of accumulation than DDB2, XPC, and RAD23B (Fig.  xref e and Supplementary Fig.  xref d)."
| PMC
sparser
"Notably, this recruitment of PSMD14-mKO1 was dependent on the presence of functional DDB2, but not XPC (Fig.  xref e)."
| PMC