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KMT2C binds BAP1. 23 / 23
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"More recently, PHD domain mutations in KMT2C were studied in human cells, revealing that these disrupt the interaction between KMT2C and the tumor suppressor BAP1."
32471474
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"In fact, the crystal structure (PDB: 2YSM) of MLL3-PHD2–3 reveals that those mutations that are important for MLL3-BAP1 complex binding, are closely associated with the zinc atoms, which help maintain the structure of PHD fingers ( xref )."
29785026
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"To investigate if the endogenous MLL3 also interacts with BAP1, we immunoprecipitated MLL3, MLL4, SET1A, and SET1B components of the COMPASS family from HEK293T cells using antibodies specific to each methyltransferase ( xref ; xref )."
29785026
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"For instance, the BAP1 H2A deubiquitinase recruits H3K4 monomethylase MLL3 to monomethylate gene enhancers, while disruption of the interaction between BAP1 and MLL3 contributes to the pathogenesis of multiple cancers [ xref ]."
31747960
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"Using a human breast cancer cell line, CAL51, we confirmed that these point mutations strongly diminish the interaction between BAP1 and MLL3-NTD ( xref )."
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"Recently identified missense mutations within the PHD fingers 1-3 have been shown to disrupt the interaction between KMT2C and BAP1 leading to reduced recruitment of KMT2C to gene enhancers 1."
30665945
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"Recently identified missense mutations within the PHD fingers 1–3 have been shown to disrupt the interaction between KMT2C and BAP1 leading to reduced recruitment of KMT2C to gene enhancers xref ."
30665945
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"In addition, a mutation hotspot within the PHD cluster of the KMT2C gene was described, the mutations of which disrupted the interaction of KMT2C with the BAP1 (BRCA1 associated protein-1) tumor suppressor, resulting in poor patient survival in many types of cancer (liver, lung, bladder, and breast)."
33302406
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"Cancer-associated MLL3 PHD mutations disrupt the interaction between MLL3 and BAP1 and correlate with poor patient survival."
29785026
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"Notably, BAP1 selectively associates with MLL3 but not with MLL4 indicating a bifurcation in the function of these complexes."
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"There are 3,858 genes associated with common MLL3, BAP1, H3K4me1 and H2Aub peaks, and all MLL3-BAP1 target genes are occupied by MLL3, BAP1 and the indicated histone marks ( xref )."
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"Cancer associated mutations in the sequence encoding the MLL3 PHD repeats disrupt the interaction between MLL3 and BAP1 and correlate with poor patient survival."
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"Mutations that inhibit MLL3-BAP1 interaction are most enriched in lung cancer, accounting for 50% cases (7 out of 14; LUSC n=3, LUAD n=4) ( xref )."
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"Western blotting analysis confirmed an interaction between the BAP1 complex and the MLL3-NTD ( xref )."
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"The interaction between BAP1 and MLL3 is largely reduced in these cells (Supplementary Fig. 10h), which is consistent with our observations in MDA-MB-453 cells."
29785026
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"More recently, PHD domain mutations in KMT2C were studied in human cells, revealing that these disrupt the interaction between KMT2C and the tumor suppressor BAP1."
32471474
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"For instance, the BAP1 H2A deubiquitinase recruits H3K4 monomethylase MLL3 to monomethylate gene enhancers, while disruption of the interaction between BAP1 and MLL3 contributes to the pathogenesis of multiple cancers [10]."
31747960
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"The interaction between BAP1 and MLL3 was also confirmed in other two additional cell lines ( xref )."
29785026
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"MLL3 COMPASS uniquely associates with the BAP1 complex."
29785026
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"Interestingly, we found that even in the heterozygous cells the interaction between MLL3 and BAP1 is largely reduced ( xref )."
29785026
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"Cancer-associated mutations in the sequence encoding the MLL3 PHD repeats disrupt the interaction between MLL3 and BAP1 and correlate with poor patient survival."
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"ASXL2 loss results in decreased MLL3 occupancy at enhancers and reduced BAP1-MLL3 target gene expression."
36197977
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"Here we report a cancer mutational hotspot in MLL3 within the region encoding its plant homeodomain (PHD) repeats and demonstrate that this domain mediates association of MLL3 with the histone H2A deubiquitinase and tumor suppressor BAP1."
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