IndraLab

Statements

KMT2C binds BAP1. 10 / 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 )."
29785026
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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."
29785026
KDM6A binds KMT2C and BAP1. 2 / 2
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"We found that cancer hotspot mutations in the MLL3 amino terminal PHD repeats disrupt its association with the BAP1 complex and result in reduced MLL3 and UTX recruitment to enhancers misregulating the epigenetic chromatin state at these loci."
29785026
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"Mutations within the MLL3 PHD domains abolish the interaction between the BAP1 tumor suppressor complex and MLL3-UTX, which leads to attenuation of enhancer activity."
30753822
KMT2C binds PDC and BAP1. 1 / 1
| 1
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"Our data suggest that MLL3 PHD-BAP1 interactions have a crucial function that is disrupted in cancer and implicate BAP1 as a previously uncharacterized regulator of MLL3 COMPASS function."
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