E3 ubiquitin-protein ligase MSL2 (MSL2)

MSL2 (E3 ubiquitin-protein ligase MSL2) is a core subunit of the human MSL complex, a multiprotein chromatin modifier essential for the regulation of transcription and histone modification[1][3]. MSL2 possesses E3 ubiquitin ligase activity, primarily monoubiquitinating histone H2B at lysine 34 in cooperation with MSL1[2]. This modification facilitates crosstalk leading to methylation of H3K4 and H3K79, activating transcription at key loci such as HOXA9 and MEIS1[2][3]. MSL2 also plays roles in dosage compensation by regulating X chromosome gene expression and contributes to DNA damage responses through ubiquitination of TP53 and TP53BP1[3]. Loss of MSL2 or disruption of its complex affects transcriptional regulation, genome integrity, and can be linked to neurodevelopmental disorders and potentially malignancy[1][2][3][4].

Other names

MSL complex subunit 2MSL2KIAA1585MSL2L1RNF184MSL2-like 1MSL-2FLJ10546msl-2Male-specific lethal 2-like 1Male-specific lethal-2 homologMale-specific lethal-2 homolog 1RING finger protein 184Male-specific lethal-2 homolog (Drosophila)KBHS

For inhibitors or modulators of MSL2 (theoretical): - Inhibition of E3 ubiquitin-protein ligase activity, thereby reducing monoubiquitination of histone H2B and affecting downstream methylation events. - Modulation of gene expression, notably genes regulated by H4K16 acetylation and H2B K34 ubiquitination