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HSF1 binds BAP1. 15 / 15
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"BAP1-HSF1 interaction inhibits the deacetylation of HSF1-K80 mediated by SIRT1, thereby promoting HSP70 mediated monomerization of HSF1 and its dissociation from target gene loci."
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"This may suggest that the binding between BAP1 and HSF1 could inhibit the ubiquitination of BAP1 mediated by UBE2O [24], or there may be other unexplored mechanisms at play."
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"Co-immunoprecipitation assays indicated that treatment with the SIRT1 inhibitor, EX-527, notably augmented the level of acetylated lysine of HFS1, as well as the interaction between HSF1 and BAP1 (Fig.  xref A)."
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"The BAP1-HSF1 interaction preserves the acetylation of HSF1-K80 and promotes HSF1-HSP70 interaction, facilitating HSF1 oligomerization and detachment from the chromatin."
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"The BAP1-HSF1 interaction safeguards the acetylation of HSF1 at the K80 site, promotes the monomerization of HSF1, and facilitates its dissociation from DNA."
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"More importantly, both wild-type (WT) and C91A mutated BAP1 attenuated the HSF1-SIRT1 interaction (Fig. 5C, Supplementary Fig. S3G), and SIRT1 knockdown resulted in an enhanced binding between HSF1 and BAP1 (Fig. 5D, Supplementary Fig. S3H), indicating that BAP1 and SIRT1 might compete with each other for binding to HSF1."
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"BAP1 interacts with the N-terminal of HSF1."
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"The subsequent Co-IP assay revealed that the N-terminal of HSF1 was pivotal for the formation of the BAP1-HSF1 complex (Fig.  xref F)."
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"Co-immunoprecipitation assays indicated that treatment with the SIRT1 inhibitor, EX-527, notably augmented the level of acetylated lysine of HFS1, as well as the interaction between HSF1 and BAP1 (Fig. 6A)."
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"Interestingly, the interaction between BAP1 and HSF1 exclusively occurs in the nucleus (Fig.  xref B)."
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"The subsequent Co-IP assay revealed that the N-terminal of HSF1 was pivotal for the formation of the BAP1-HSF1 complex (Fig. 3F)."
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"Interestingly, the interaction between BAP1 and HSF1 exclusively occurs in the nucleus (Fig. 4B)."
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"Despite BAP1 inhibiting the trimerization of HSF1 by enhancing the interaction between HSP70 and HSF1, the BAP1-HSF1 interaction remains unaffected by HSP70 (Fig.  xref G), suggesting the existence of a potential mechanism for BAP1 to interact with HSF1 and subsequently recruit HSP70 to monomerize HSF1."
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"Considering SIRT1 promotes HSF1 activity via the deacetylation at K80 of HSF1 [ xref ], We constructed the acetylation resistant mutant (HSF1(K80R)) and acetylation mimic mutant (HSF1(K80Q)) to further investigate how HSF1-K80 acetylation influence HSF1-BAP1."
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"Co-IP assay indicated that BAP1 exhibited remarkably enhanced interaction with HSF1(K80Q) mutant compared to WT HSF1, while the acetylation resistant mutation (HSF1(K80R)) almost abolished HSF1-BAP1 interaction (Fig.  xref E, Supplementary Fig. xref I)."
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