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Details on Person "MOF (males absent on the first) is a histone H4 acetyltrans...
| Class:Id | Summation:9770950 |
|---|---|
| _displayName | "MOF (males absent on the first) is a histone H4 acetyltrans... |
| _timestamp | 2022-04-18 12:04:43 |
| created | [InstanceEdit:9770951] Orlic-Milacic, Marija, 2022-04-18 |
| literatureReference | [LiteratureReference:9770958] The Functional Analysis of Histone Acetyltransferase MOF in Tumorigenesis [LiteratureReference:3321809] A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16 [LiteratureReference:3321891] Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila [LiteratureReference:3321879] Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex [LiteratureReference:9770949] The nonspecific lethal complex is a transcriptional regulator in Drosophila [LiteratureReference:9770960] Structural analysis of the KANSL1/WDR5/KANSL2 complex reveals that WDR5 is required for efficient assembly and chromatin targeting of the NSL complex [LiteratureReference:9770968] Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF [LiteratureReference:9770965] Crosstalk between NSL histone acetyltransferase and MLL/SET complexes: NSL complex functions in promoting histone H3K4 di-methylation activity by MLL/SET complexes |
| modified | [InstanceEdit:9770973] Orlic-Milacic, Marija, 2022-04-18 |
| text | "MOF (males absent on the first) is a histone H4 acetyltransferase that assembles into two distinct functional complexes, the MSL (male-specific lethal) complex and the non-specific lethal (NSL) complex (reviewed in Su et al. 2016). WDR5 associates with MOF only within the NSL complex (Smith et al. 2005; Mendjan et al. 2006; Cai et al. 2010; Raja et al. 2010), which also includes five other subunits: KANSL1, KANSL2, KANSL3, PHF20, and MCRS1 (Mendjan et al. 2006; Cai et al. 2010; Raja et al. 2010). Direct interaction of WDR5 with components of the NSL complex are parallel and mutually exclusive with direct interactions in the SET1/MLL complexes. WDR5 directly interacts with KANSL2 and with KANSL1 at the same exact binding sites that bind RBBP5 (WBM site) and SET1/MLL enzymes (Win site), respectively. The region of KANSL2 that binds WDR5 is highly conserved and contains a WBM motif that is parallel to the WBM of RBBP5. Similarly, KANSL1 binds to WDR5 through a highly conserved arginine-containing Win motif, analogous to the Win motifs within H3 and the SET1/MLL proteins. At least in Drosophila, this KANSL1-WDR5 interaction appears to be required for efficient recruitment of the NSL complex to chromatin (Dias et al. 2014)." "The NSL complex may function to boost SET1/MLL methyltransferase activity, pointing to a crosstalk between these two varieties of histone modifying complexes (Dou et al. 2005; ." |
| (summation) | [Reaction:9770959] Formation of the NSL complex [Homo sapiens] |
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