IndraLab

Statements


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sparser
"Together, our data suggested a model that the BAP1-containing PR-DUB complex binds on the S LC7A11 promoter, where BAP1 removes ubiquitin from H2Aub, and BAP1-dependent H2Aub reduction on SLC7A11 is associated with BAP1-mediated SLC7A11 repression."

sparser
"Our results reveal that the physiological modulation of BAP1 determines the invasive properties of the trophoblast, delineating a new role of the BAP1 PR-DUB complex in regulating early placentation."

sparser
"These BAP1 mutants did not significantly affect BAP1’s interaction with other components of the PR-DUB complex ( xref )."

sparser
"The N-terminal PHD region of MLL3/KMT2C has been shown to bind the BAP1-containing PR-DUB complex, which is also a tumor suppressor and acts as a deubiquitinase for histone H2A."

sparser
"Similar to ASXL1, ASXL2 forms a stable and distinct PR-DUB complex with BAP1, promoting ubiquitin removal from histone H2A. However, unlike ASXL1, ASXL2 is stabilized by BAP1 [ xref , xref ], indicating the existence of additional regulatory mechanisms."

sparser
"In human cells, ASXL3 protein was shown to interact with BAP1 to form the PR-DUB complex ( xref )."

sparser
"The BAP1-PR-DUB interaction was confirmed in PLC cells by coimmunoprecipitation (fig."

sparser
"Truncated ASXL1 mutants, specifically the ASXL1 fragment containing amino acids 1–587, drive myeloid transformation by forming a stable PR-DUB complex with BAP1, thereby enhancing BAP1 deubiquitinase activity [ xref , xref , xref ]."

sparser
"Truncated ASXL1 mutants promote myeloid transformation by creating a potent PR-DUB complex with BAP1 [ xref , xref , xref ]."

sparser
"BAP1 PR-DUB complex is also regulated during human trophoblast differentiation."

sparser
"Polycomb group complexes, including the BAP1 PR-DUB, are well conserved throughout evolution ( xref ), leading to the question whether BAP1 also functions to regulate trophoblast differentiation and invasion during human placentation."

sparser
"Intriguingly, ASXL3, similar to ASXL1 and ASXL2, forms a PR-DUB complex with BAP1 but also exclusively interacts with BRD4, which binds to acetylated histones via its bromodomains in small cell lung carcinoma [ xref ]."