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USP49 deubiquitinates H2AX. 7 / 7
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"These results suggested that over-expression of USP49 suppressed phleomycin-induced γH2AX ubiquitylation in a DUB activity dependent manner."
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"These results suggest that USP49 negatively regulates ubiquitylation of γH2AX not in a ZnF-UBP domain but a DUB activity dependent manner.To further understand the involvement of USP49 in DDR, we exam[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In addition, we found that USP49 negatively regulates DSB-induced γH2AX ubiquitylation ( Fig. 1 B)."
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"1) Over-expression of USP49 suppressed DSB-induced ubiquitylation of γH2AX in its catalytic activity dependent manner."
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"This could suggest that USP49 suppresses 53BP1 binding to chromatin by deubiquitylating γH2AX when cells were not challenged."
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"Phleomycin treatment induced ubiquitylation of γH2AX that was suppressed by the transient over-expression of GFP-USP49 (WT) in comparison to GFP expression ( Fig. 1 B)."
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"Contrary, γH2AX ubiquitylation was not suppressed by the transient over-expression of a catalytically inactive mutant GFP-USP49 [GFP-USP49 (CA)] in which Cys262 was replaced with Ala ( Fig. 1 B) ( Zha[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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