IndraLab

Statements

UBR5 ubiquitinates OTUD5. 8 / 8
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"UBR5-dependent ubiquitylation of OTUD5 was almost completely diminished with TRIP12 knockdown (Fig. 2g, lanes 2 and 4), whereas TRIP12-dependent ubiquitylation was partially decreased by UBR5 knockdown (Fig. 2h, lanes 2 and 4, and supplementary Fig. 1d)."
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"UBR5-dependent ubiquitylation of OTUD5 was almost completely diminished with TRIP12 knockdown (Fig.  xref , lanes 2 and 4), whereas TRIP12-dependent ubiquitylation was partially decreased by UBR5 knockdown (Fig.  xref , lanes 2 and 4, and supplementary Fig.  xref )."
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"Notably, UBR5 ubiquitylation of wild-type OTUD5 was less effective than that of C224R OTUD5 (Fig. 5b (i))."
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"The data on a catalytically-inactive OTUD5 (Fig.  xref ) suggest that the ubiquitylation of OTUD5 by TRIP12 and UBR5 appears as if they act sequentially because OTUD5 DUB activity negates UBR5 activity, which is different from typical chain initiation (priming)-elongation model xref , xref ."
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"Since UBR5 can stably associate with OTUD5 xref , UBR5 may transiently ubiquitylate OTUD5 with K48-linked chains."
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"The data on a catalytically-inactive OTUD5 (Fig. 5) suggest that the ubiquitylation of OTUD5 by TRIP12 and UBR5 appears as if they act sequentially because OTUD5 DUB activity negates UBR5 activity, which is different from typical chain initiation (priming)-elongation model ."
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"Next, we investigated whether OTUD5 DUB activity counteracted OTUD5 ubiquitylation by TRIP12 or UBR5."
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"Notably, UBR5 ubiquitylation of wild-type OTUD5 was less effective than that of C224R OTUD5 (Fig.  xref (i))."
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