IndraLab

Statements

ASXL1-MT binds BAP1. 13 / 13
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"This hyperactive ASXL1-MT and BAP1 complex promotes aberrant myeloid differentiation of haematopoietic progenitor cells and accelerates RUNX1-ETO-driven leukaemogenesis."
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"In immunoprecipitation assays, BAP1 interacted with ASXL1-MT and induced its monoubiquitination."
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"Together, these results indicate that the ASXL1-MT and BAP1 complex impairs terminal differentiation of HSPCs, except for differentiation toward monocytes."
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"Cells expressing ASXL1-MT and BAP1 did not produce colonies beyond the fourth passage, suggesting that the ASXL1-MT and BAP1 complex itself is not sufficient to transform murine HSPCs."
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"To examine the cooperation between ASXL1-MT and BAP1 in human RUNX1-ETO cells, we transduced ASXL1-MT or ASXL1-MT-K351R (coexpressing GFP) together with BAP1 or BAP1-C91S (coexpressing NGFR), and monitored changes of the frequency of the GFP + NGFR + double positive fraction in culture."
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"Thus, Irf8 is also a downstream target of the ASXL1-MT and BAP1 complex, which is likely to underlie the enhanced monocytic differentiation of HSPCs coexpressing ASXL1-MT and BAP1."
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"These data indicate that the ASXL1-MT and BAP1 complex induces upregulation of posterior HOXA genes and IRF8 via removal of H2AK119ub."
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"In addition to these reports implicating BAP1 in myeloid transformation, the present results identify the underlying molecular mechanisms by which ASXL1-MT and BAP1 complex induce myeloid transformation; BAP1 plays a necessary role in maintaining aberrant posterior HOXA expression in ASXL1-mutant leukemia and in sustaining their leukemic proliferation."
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"The ASXL1-MT and BAP1 complex enhances transient myeloid proliferation, but does not increase the long-term proliferation potential of murine and human HSPCs."
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"The ASXL1-MT and BAP1 complex is not a simple growth-accelerator, but rather inhibits terminal differentiation of HSPCs toward granulocytes, macrophages, mast cells, and erythrocytes."
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"We also identified IRF8, a master regulator of monocyte differentiation, as a novel target gene of the ASXL1-MT and BAP1 complex."
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"Monoubiquitinated ASXL1-MT in turn enhances the catalytic activity of BAP1, creating a positive feedback loop that establishes the hyperactive ASXL1-MT and BAP1 complex."
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"Mechanisms underlying the enhancement of the catalytic activity of ASXL1-MT and BAP1 complex warrant further investigation."
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