Редактирование: BAP1

Ubiquitin carboxyl-terminal hydrolase BAP1 (EC 3.4.19.12) (BRCA1-associated protein 1) (Cerebral protein 6) [KIAA0272] [hucep-6]

==Publications==

{{medline-entry
|title=The [[BAP1]]/[[ASXL2]] Histone H2A Deubiquitinase Complex Regulates Cell Proliferation and Is Disrupted in Cancer.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/26416890
|abstract=The deubiquitinase (DUB) and tumor suppressor [[BAP1]] catalyzes ubiquitin removal from histone H2A Lys-119 and coordinates cell proliferation, but how [[BAP1]] partners modulate its function remains poorly understood. Here, we report that [[BAP1]] forms two mutually exclusive complexes with the transcriptional regulators [[ASXL1]] and [[ASXL2]], which are necessary for maintaining proper protein levels of this DUB. Conversely, [[BAP1]] is essential for maintaining [[ASXL2]], but not [[ASXL1]], protein stability. Notably, cancer-associated loss of [[BAP1]] expression results in [[ASXL2]] destabilization and hence loss of its function. [[ASXL1]] and [[ASXL2]] use their ASXM domains to interact with the C-terminal domain (CTD) of [[BAP1]], and these interactions are required for ubiquitin binding and H2A deubiquitination. The deubiquitination-promoting effect of ASXM requires intramolecular interactions between catalytic and non-catalytic domains of [[BAP1]], which generate a composite ubiquitin-binding interface (CUBI). Notably, the CUBI engages multiple interactions with ubiquitin involving (i) the ubiquitin carboxyl hydrolase catalytic domain of [[BAP1]], which interacts with the hydrophobic patch of ubiquitin, and (ii) the CTD domain, which interacts with a charged patch of ubiquitin. Significantly, we identified cancer-associated mutations of [[BAP1]] that disrupt the CUBI and notably an in-frame deletion in the CTD that inhibits its interaction with [[ASXL1]]/2 and DUB activity and deregulates cell proliferation. Moreover, we demonstrated that [[BAP1]] interaction with [[ASXL2]] regulates cell senescence and that [[ASXL2]] cancer-associated mutations disrupt [[BAP1]] DUB activity. Thus, inactivation of the [[BAP1]]/[[ASXL2]] axis might contribute to cancer development. 
|mesh-terms=* Cell Proliferation
* HEK293 Cells
* HeLa Cells
* Histones
* Humans
* Multiprotein Complexes
* Neoplasms
* Repressor Proteins
* Tumor Suppressor Proteins
* Ubiquitin Thiolesterase
* Ubiquitin-Specific Proteases
|keywords=* ASXL
* BAP1
* Calypso
* Polycomb Group Proteins
* cancer biology
* cell proliferation
* cellular senescence
* deubiquitylation (deubiquitination)
* epigenetics
* histone H2A ubiquitination
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4661380
}}
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