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USP11 deubiquitinates KLF4. 4 / 4
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"25 , 26 , 27 Recently, USP11 was shown to promote HCC development, 28 but the underlying molecular mechanisms involved in this pathogenic process remain poorly understood.In this study, we used a proteomic approach to identify KLF4‐interacting DUBs and firstly discovered that USP11 was responsible for deubiquitinating KLF4 in HCC cells."
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"These results demonstrate that the ID domain of KLF4 and the catalytic domain of USP11 are responsible for KLF4‐USP11 interaction.Next, we investigated whether USP11 could deubiquitinate KLF4 as a DUB."
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"USP11 deubiquitinates K63‐dependent polyubiquitination of KLF4 and suppresses its stability."
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"The results suggested that coexpression of USP11 and KLF4 significantly prevented the ubiquitination of KLF4 mediated by WT‐Ub, but not from KO‐Ub (Figure 2A)."
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