IndraLab

Statements

MBD5 binds MBD6 and BAP1. 8 / 8
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"Furthermore, we have demonstrated that MBD5 or MBD6 do not directly interact with BAP1; instead, they bind to the C-terminal PHD fingers of all three ASXL subunits (ASXL1-3)."
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"This result indicates an indirect interaction between MBD5, MBD6, and BAP1."
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"To determine whether MBD5 and MBD6 can also bind to chromatin similar to other BAP1 subunits, we conducted Chromatin Immunopreciptiation Sequencing (ChIP-seq) and determined the chromatin binding profiles of MBD5 and MBD6 with our validated homemade antibodies (Additional file xref : Fig. S1F)."
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"To investigate how MBD5 and MBD6 subunits are incorporated into the BAP1 complex, we first hypothesized that MBD5 and MBD6 may directly interact with BAP1 itself, similar to how other subunits function (e.g., ASXL1-3 and FOXK1/2)."
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"Therefore, to determine whether ASXLs play a role in mediating the interaction between MBD5, MBD6, and BAP1, we knocked out all three ASXL genes (TKO) by CRISPR in HEK293T cells."
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"Surprisingly, as shown in Fig. xref B, the protein-protein interaction between MBD5, MBD6, and BAP1 is completely abolished in ASXL-TKO cells (Fig. xref B)."
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"Therefore, MBD5 and MBD6 have been excluded from the BAP1 complex due to a lack of evidence on endogenous protein-protein interaction between MBD5, MBD6, and BAP1 [ xref , xref – xref ]."
36180891
sparser
"After testing the specificity of the antibodies, we performed immunoprecipitation in HEK293T cells and demonstrated a stable protein-protein interaction between endogenous MBD5, MBD6, and BAP1 (Fig. xref C, D)."
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