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OTUD7B deubiquitinates KDM1A. 8 / 9
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"For example, high OTUD7B expression in breast cancer acts to deubiquitinate LSD1, in turn activating histone deacetylase complexes to promote metastasis through epigenetic effects 19."
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"OTUD7B Deubiquitinates LSD1 to Govern Its Binding Partner Specificity, Homeostasis, and Breast Cancer Metastasis."
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"As shown in Figure S3A in the Supporting Information, K63R mutation caused significant loss of polyubiquitinated LSD1 signals, whereas K48R displayed very marginal reduction in LSD1 ubiquitination, suggesting LSD1 ubiquitination involves mixed linkage specificity, and predominantly prefers K63‐linked polyubiquitin chains.We next determined whether OTUD7B modulated LSD1 deubiquitination."
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"Conversely, OTUD7B depletion remarkably enhanced polyubiquitination of endogenous LSD1 (Figure 2B)."
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"To assess the types of Ub‐linkage that OTUD7B may catalyze when deubiquitinates LSD1, we utilized two Ub mutants, K48 and K63."
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"Ubiquitin-specific peptidase 7 (USP7) and OTU deubiquitinase 7B (OTUD7B) mediate the deubiquitylation and stability of LSD1, which is crucial for breast cancer invasion and metastasis [ 13 , 14 ]."
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"Therefore, perturbation of OTUD7B–LSD1 axis results in changes in both activating and repressive chromatin modification marks, providing a plausible mechanism for altered gene transcription due to OTUD7B loss.To investigate the contribution of LSD1 deubiquitination by OTUD7B in OTUD7B‐mediated LSD1 genomic distribution and H3K4me2/H3K9me2 enrichment, we analyzed LSD1 binding and H3K4me2/H3K9me2 levels of the selected 11 genes in LSD1 reconstituting cells."
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"The OTUD7B is responsible for the deubiquitination of LSD1 at the K226/277 residues, and OTUD7B depletion increases the LSD1 K63‐linked ubiquitination and p62‐mediated proteolysis [40]."
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